Crystal Structures Of O-glcnac Transferase And Uses Thereof

Crystal Structures of O-GlcNAc Transferase and Uses Thereof

RELATED APPLICATIONS

[0001] This application claims priority under 35 U.S.C. § 119(e) to U.S. Provisional

Patent Application, U.S. S.N. 61/403,258, filed September 13, 2010, which is incorporated herein by reference.

GOVERNMENT SUPPORT

[0002] This invention was made with U.S. Government support under GM076710 awarded by National Institutes of Health. The U.S. Government has certain rights in the invention.

BACKGROUND

[0003] The hexosamine biosynthetic pathway (HSP) is a minor branch of the glycolytic pathway, diverting 3-5% of cellular glucose toward the synthesis of UDP-GlcNAc, which is either transported to the Golgi and used in the synthesis of complex glycans or remains in the cytoplasm where it is the substrate for O-GlcNAc transferase (OGT). OGT is the sole known enzyme to catalyze the glycosylation of serine and threonine residues on many nuclear and cytoplasmic proteins (termed O-GlcNAcylation). This post-translational modification is dynamic and is a general mechanism, like protein phosphorylation, of signal transduction.

[0004] Excess flux through the HSP has been implicated in both the early (insulin resistance) and late (nephropathy, microvascular damage) stages of diabetes mellitus. Diabetes involves a deficiency in the availability and/or utilization of insulin. Insulin is a hormone produced by the pancreas and is necessary for cells to utilize glucose. Insulin resistance is a condition in which muscle, fat, and liver cells do not use insulin properly. As a result, the pancreas produces more insulin, which is also not used properly. Eventually, the pancreas cannot keep up with the body's need for insulin, and excess glucose builds up in the

bloodstream. Thus, in insulin resistance, there may be high levels of blood glucose and high levels of insulin circulating in the bloodstream at the same time.

[0005] Experiments have shown that insulin resistance due to increased hexosamine flux is caused by hyper O-GlcNAcylation. Diabetic patients have increased production of two adipokines directly responsible for vascular injury, plasminogen activator inhbitor-1 (PAI-1) and transforming growth factor βΐ (TGF-βΙ). Transcription of both of these proteins is decreased in cell culture when levels of O-GlcNAcylation are decreased. The molecular mechanism for this is known; increased transcription is mediated by the O-GlcNAcylation state of the transcription factor Spl.

[0006] OGT is an essential mammalian enzyme that couples metabolic status to the regulation of a wide variety of cellular signaling pathways by acting as a nutrient sensor 1 ' 2. The ability to sense and respond to nutrient levels is critical for the growth of all living systems. OGT senses cellular glucose levels via UDP-GlcNAc concentrations and responds by dynamically O-GlcNAcylating a wide range of nuclear and cytoplasmic proteins.1'14 These include proteins involved in insulin-like signaling pathways10 and transcriptional activators that regulate glucose levels by controlling gluconeogenesis.15 Since many known O-GlcNAcylation sites are also phosphorylation sites, OGT is proposed to play a major role in modulating cellular kinase signaling cascades.16 It has also been shown that OGT is involved in widespread transcriptional regulation.17"19

[0007] OGT catalyzes the transfer of N-acetyl-glucosamine from UDP-GlcNAc to serines and threonines of cytoplasmic, nuclear and mitochondrial proteins3'4, including numerous transcription factors5, tumor suppressors6, kinases7, phosphatases8, and histone-modifying proteins9. Prolonged hyperglycemia, such as occurs in diabetes, or excessive glucose uptake, such as occurs in cancer cells, results in hyper-O-GlcNAcylation of cellular proteins by OGT, and this increased O-GlcNAcylation has been linked to harmful cellular effects 20. Aberrant O- GlcNAcylation by OGT has been linked to, for example, insulin resistance10, diabetic complications 11 , cancer12 and neurodegenerative diseases including Alzheimer's 13. Despite the importance of OGT, the details of how the enzyme recognizes its protein substrates are largely unknown and the lack of a crystal structure of OGT has been a major impediment to developing inhibitors, to understanding substrate recognition, and to exploring OGT's molecular

mechanisms.

[0008] Therefore, a better understanding of OCT and its catalysis of O-GlcAcylation may aid in the development of better treatment for diabetes and other metabolic diseases. SUMMARY OF THE INVENTION

[0009] The invention relates to x-ray crystal structures of human O-GlcNAc transferase

(OGT). The present invention provides methods for crystallizing human OGT and variants thereof; x-ray crystal structures of human O-GlcNAc transferase (OGT) as a binary complex with UDP (2.8 A) and a ternary complex with UDP and a peptide substrate (1.95 A); and methods of using these crystal structures. The x-ray crystal structures provided herein illuminate aspects of the enzyme mechanism, provide information on how OGT recognizes target peptide sequences, and reveal the fold of a unique domain between the two halves of the catalytic region. Such information may be useful in designing, identifying, and/or screening compounds that bind to OGT, such as OGT inhibitors or activators.

[0010] Other aspects of the invention relate to providing OGT structural information enabling the rational design of biological experiments to investigate OGT's functions and the rational (in silico) design of modulators of OGT activity.

[0011] Other aspects of the invention relate to screening methods for novel inhibitors of

OGT activity using the structural information of OGT provided herein. Novel compounds identified by the methods provided herein may be used to inhibit O-GlcNAc transferase (OGT) activity. O-GlcNAcylation by OGT is the glycosylation of serine and/or threonine residues on nuclear and cytoplasmic proteins that is catalyzed by OGT. Aberrant activity of OGT has been linked to disease. For example, prolonged hyperglycemia, such as that which occurs in diabetes, or excessive glucose uptake, such as occurs in cancer cells, results in hyper- O-GlcNAcylation of cellular proteins by OGT, and this increased O-GlcNAcylation has been linked to harmful cellular effects. 20 OGT inhibitors identified by the methods described herein may be useful for the treatment of diseases associated with hyper-O-GlcNAcylation. In certain embodiments, diseases associated with hyper-O-GlcNAcylation are diabetes, proliferative diseases (e.g. cancer, benign neoplasms, hyperplasias, etc.), neurodegenerative diseases, autoimmune diseases, and inflammatory diseases. Any binding compounds (such as inhibitors, activators, etc.) may be designed in silico based on the three dimensional structural information provided by the atomic coordinates described herein. OGT binding compounds may also be useful for other applications, such as scientific research, e.g. in biological experiments to investigate OGT's functions or as stabilizing agents in crystallography (e.g. in co-crystallization experiments). [0012] Provided herein are methods of identifying a binding compound of O-linked N- acetylglucosamine transferase (OGT). In certain embodiments, OGT is mammalian. In a specific embodiment, OGT is human. In another embodiment, OGT is mutant OGT, such as a naturally occurring mutant. In certain embodiments, OGT is a variant, such as a splice variant, isoform, or ortholog of human OGT. In certain embodiments, the OGT is 80%, 90%, 95%, 98%, or 99% homologous to OGT comprising the amino acid sequences of SEQ ID NO: 53 or 54. The methods provided herein may include computationally identifying a binding compound that binds to OGT using the atomic coordinates of amino acids H498 and K842 as set forth in Tables 5, 6, or 7 and may further include using the atomic coordinates of one or more of amino acids D431, N458, H499, D523, H558, T560, R637, L653, Q839, K842, K898, H901, H920, T921, and D925. Optionally, the step of computationally identifying may include designing in silico a binding compound that binds to OGT. Such binding compound may be designed from a known compound.

[0013] Further provided herein are methods of identifying a binding compound of O-linked N-acetylglucosamine transferase (OGT) wherein the methods include (a) providing a set of atomic coordinates for a OGT polypeptide as set forth in Table 5, 6, or 7; and (b) identifying in silico a binding compound that binds to OGT using the coordinates of (a). In certain

embodiments, the identified binding compound is a modulator of OGT activity, such as an inhibitor of OGT activity.

[0014] Further provided herein are methods of identifying a drug candidate for the treatment of a disease wherein the methods include a) using the atomic coordinates set forth in Table 5, 6, or 7 to form a three-dimensional structure of OGT; b) selecting a test compound having the best fit with the structure of OGT; and c) assaying the ability of the test compound to modulate OGT activity, wherein a test compound that modulates OGT activity is considered a drug candidate for treating a disease. The disease may be a proliferative disease {e.g., a cancer, benign neoplasm), a neurodegenerative disease, an autoimmune disease, an inflammatory disease, a metabolic disease, or diabetes.

[0015] In certain embodiments, the binding compound identified by the methods described herein is a modulator of OGT activity, such as an inhibitor of OGT activity.

Optionally, binding compounds identified by the methods described herein are tested for their binding to OGT and/or tested for their ability to modulate (e.g. inhibit) OGT activity. The binding compound may be an OGT catalytic substrate or a derivative thereof, such as for example a UDP or UDP-GlcNAc derivative or the binding compound may be a polypeptide, such as the polypeptides set forth in Table 4. Such binding polypeptides, in certain embodiments, may be modified, for example, they may contain one or more amino acid substitutions, such as a conservative amino acid substitution; a substitution with a non-natural amino acid, or a substitution with a pseudopeptide unit. In certain embodiments, the binding compound identified by the methods described herein can be a peptidomimetic or a small molecule, such as a small molecule that comprises a quinolinone or dihdyroquinolinone core. In certain embodiments, such small molecule binding compounds may comprises formula (I):

(I)

wherein:

= denotes a single or double bond;

R1 is cyclic or acyclic, substituted or unsubstituted, branched or unbranched aliphatic; cyclic or acyclic, substituted or unsubstituted, branched or unbranched heteroaliphatic; substituted or unsubstituted aryl; substituted or unsubstituted heteroaryl; substituted or unsubstituted, branched or unbranched arylalkyl; or substituted or unsubstituted, branched or unbranched heteroarylalkyl;

2 3

and RJ are independently hydrogen; cyclic or acyclic, substituted or unsubstituted, branched or unbranched aliphatic; cyclic or acyclic, substituted or unsubstituted, branched or unbranched heteroaliphatic; substituted or unsubstituted, branched or unbranched acyl;

substituted or unsubstituted aryl; substituted or unsubstituted heteroaryl; substituted or unsubstituted, branched or unbranched arylalkyl; substituted or unsubstituted, branched or

B B B B

unbranched heteroarylalkyl; -C(=0)R ; -SOR ; -S02R ; or -C(R )3; wherein each occurrence of R is independently hydrogen; halogen; a protecting group; aliphatic; heteroaliphatic; acyl; aryl; heteroaryl; alkoxy; aryloxy; amino; alkylamino; dialkylamino; or heteroaryloxy; or

2 3

R" and RJ may optionally be taken together with the intervening nitrogen to form a saturated or unsaturated, substituted or unsubstituted heterocyclic moiety;

R4 is hydrogen, C1-6 aliphatic, or a protecting group; R5 is hydrogen, C1-6 aliphatic, or a protecting group;

R6 is hydrogen; halogen; cyclic or acyclic, substituted or unsubstituted, branched or unbranched aliphatic; cyclic or acyclic, substituted or unsubstituted, branched or unbranched heteroaliphatic; substituted or unsubstituted, branched or unbranched acyl; substituted or unsubstituted, branched or unbranched aryl; substituted or unsubstituted, branched or unbranched heteroaryl; -ORF; -C(=0)RF; -C02RF; -C(=0)N(RF)2; -CN; -SCN; -SRF; -SORF; -S02RF; -N02; -

F F F F

N(R")2; -NHC(0)R"; or -C(Rr)3; wherein each occurrence of R is independently hydrogen; halogen; a protecting group; aliphatic; heteroaliphatic; acyl; aryl moiety; heteroaryl; alkoxy; aryloxy; alkylthioxy; arylthioxy; amino; alkylamino; dialkylamino; heteroaryloxy; or heteroarylthioxy; and

n is 0, 1, 2, or 3; and pharmaceutically acceptable salts thereof.

[0016] In certain embodiments, the atomic coordinates of OGT used in the methods described herein are derived from a co-crystal of OGT and uridine diphosphate (UDP). In other embodiments, the atomic coordinates of OGT used in the methods described herein are derived from a co-crystal of OGT, UDP, and a binding peptide, such as is set forth in Table 4 or a modified form thereof. In a specific embodiment, the binding peptide is YPGGSTPVSSANMM (SEQ ID NO: 1).

[0017] Further provided herein are methods of identifying a binding compound of O-linked N-acetylglucosamine transferase (OGT) wherein the methods include computationally identifying a binding compound that binds to OGT using the atomic coordinates as set forth in Table 5, 6, or 7, wherein the atomic coordinates comprise on or more of: a) the C-Cat domain (amino acids 828-997), b) the N-Cat domain (amino acids 496-697), c) the Int-D domain (amino acids 698-827), d) a tetratricopeptide repeat (TPR) unit, or a portion or combination of any of the domains or units of (a) to (d). In certain embodiments, the TRP unit in (d) comprises one-half, one, two, three, four, five, six, seven, eight, nine, ten, eleven, twelve, or thirteen TPR units.

[0018] Further provided herein are methods of identifying a binding compound of O-linked N-acetylglucosamine transferase (OGT) wherein the methods include computationally identifying a binding compound that binds to OGT using the atomic coordinates as set forth in Table 5, 6, or 7, wherein the atomic coordinates comprise one or more of amino acids: 1-1028, 1-997, 1-828, 1-827, 1-698, 1-697, 1-496, 167-1028, 167-997, 167-828, 167-827, 167-698, 167- 697, 167-496, 313-1028, 313-997, 313-828, 313-827, 313-698, 313-697, 313-496, 372-1028, 372-997, 372-828, 372-827, 372-698, 372-697, 372-496, 466-1028, 466-997, 466-828, 466-827, 466-698, 466-697, 466-496, 496-1028, 496-997, 496-828, 496-827, 496-698, 496-697, 697- 1028, 697-997, 697-828, 697-827, 698-1028, 698-997, 698-828, 698-827, 827-1028, 827-997, 828-1028, 828-997, and 997-1028, as set forth in Figure 1A.

[0019] Further provided herein are methods of identifying a binding compound of O-linked N-acetylglucosamine transferase (OGT) wherein the methods include computationally identifying a binding compound that binds to OGT using the atomic coordinates as set forth in Table 5, 6, or 7, wherein the atomic coordinates comprise amino acids 313-1028 (SEQ ID NO: 54).

[0020] Further provided herein are methods for the design and identification of a potential binding compound for human O-linked N-acetylglucosamine transferase (OGT) wherein the methods include the steps of: (a) generating, on a computer, a three-dimensional structure of OGT having the structural coordinates of Table 5, 6, or 7; (b) identifying amino acid residues forming an OGT active site from the three-dimensional structure of OGT from step (a) in order to generate a three-dimensional model of the OGT active site, wherein the OGT active site comprises amino acids H498 and K842 according to Table 5, 6, or 7; (c) designing and/or selecting a compound that potentially binds to the OGT active site using the three-dimensional model of the OGT active site; and (d) synthesizing and/or choosing the potential binding compound. Optionally, the methods further include the steps of: (e) contacting the potential binding compound with OGT in the presence of an O-linked N-acetylglucosamine (O-GlcNAc) acceptor; and (f) determining the percent inhibition of O-GlcNAc transferase activity of OGT. Such methods may also include using the atomic coordinates of one or more of amino acids D431, N458, H499, D523, H558, T560, R637, L653, Q839, K842, K898, H901, H920, T921, and D925. In certain embodiments, the O-GlcNAc acceptor is a polypeptide, such as is set forth in Table 4.

[0021] Further provided herein are computer-assisted methods for identifying potential OGT polypeptide binding compounds, using a programmed computer comprising a processor, a data storage system, an input device, and an output device, wherein the methods include a) inputting into the programmed computer through said input device data comprising the atomic coordinates of a subset of the atoms generated from a complex of OGT and a binding compound, thereby generating a criteria data set; b) comparing, using said processor, said criteria data set to a computer database of chemical structures stored in said computer data storage system; c) selecting from said database, using computer methods, chemical structures having a portion that is structurally similar to said criteria data set; and d) outputting to said output device the selected chemical structures having a portion similar to said criteria data set. The subsets of atomic coordinates used in such methods may include one or more of amino acids D431, N458, H498, H499, H558, R637, Q839, Y841, K842, K898, and H901, and optionally one or more of amino acids D523, T560, L653, H920, T921, and D925 as set forth in Table 5, 6, or 7.

[0022] Further provided herein are computer readable media that include the atomic coordinates of OGT as set forth in Tables 5, 6, or 7 and may optionally further include programming for displaying a molecular model of OGT, programming for identifying a binding compound to OGT, and/or a database of structures of drug candidates. Further provided herein are computer systems that include such computer-readable media.

[0023] Further provided herein are computer systems that include a memory unit comprising atomic coordinates defining OGT as set forth in Table 5, 6, or 7; and a processor in electrical communication with the memory unit; wherein the processor generates a molecular model having a three dimensional structure representative of at least a portion of OGT.

[0024] Further provided herein are computer systems that include a memory unit comprising atomic coordinates of amino acids H498 and K842 of OGT as set forth in Table 5, 6, or 7; and a processor in electrical communication with the memory unit; wherein the processor generates a molecular model having a three dimensional structure representative of at least a portion of OGT. The memory unit may optionally further comprise the atomic coordinates of one or more of amino acids D431, N458, H499, H558, R637, Q839, Y841, K898, H901 and further optionally one or more of amino acids D523, T560, L653, H920, T921, and D925 as set forth in Table 5, 6, or 7.

[0025] Further provided herein are crystals, crystallizable compositions, and crystal structures of O-linked N-acetylglucosamine transferase (OGT). In certain embodiments, the crystal, crystallizable composition, or crystal structure is obtained from mammalian OGT, such as human OGT. In certain embodiments, crystals, crystallizable compositions, or crystal structures provided include OGT that is complexed with a binding compound. In certain embodiments, the binding compound is a polypeptide, such as is set forth in Table 4. In another embodiment, the binding compound is UDP, UDP-GlcNAc, or a derivative thereof. The crystals, crystallizable compositions, and crystal structures provided herein may include OGT that is co-crystallized with UDP or OGT that is co -crystallized with UDP and a binding polypeptide. In certain embodiments, the binding polypeptide comprises YPGGSTPVSSANMM (SEQ ID NO: 1). In a specific embodiment, the binding peptide is YPGGSTPVSSANMM (SEQ ID NO: 1). In another embodiment, the binding peptide is at least 90%, 95%, 98%, or 99% homologous to YPGGSTPVSSANMM (SEQ ID NO: 1). In certain embodiments, the crystal structures provided have a space group P321 and unit cell parameters a=b=273.6592 A, c=143.0501 A and bond angles α=β= 90°, γ=120°. In other embodiments, , the crystal structures provided have a space group 1121 and a unit cell parameters a=98.538 A, b=136.66 A, c=153.54 A and bond angles α= γ=90°, β= 102.90°.

This application refers to various issued patents, published patent applications, journal articles, and other publications, all of which are incorporated herein by reference. DEFINITIONS

[0026] The "active site" of an enzyme refers to the catalytic site of the enzyme (i.e. , where the reaction catalyzed by the enzyme occurs). The structure and chemical properties of the active site typically allow the recognition and binding of a substrate. The active site typically includes residues responsible for the binding specificity (e.g., charge, hydrophobicity, and/or steric hindrance) and catalytic residues of the enzyme. The term "active site," as used herein, comprises, for example, the following sites in OGT: a site where the UDP moiety binds and a site where the peptide substrate binds (examples are provided in Table 4). The catalytic region contains three domains: the N-terminal domain (N-Cat), the C-terminal domain (C-Cat), and an intervening domain (Int-D). The N-Cat domain contains two helices that form an essential part of the active site. The intervening sequence folds into a novel domain that packs exclusively against the C-Cat domain. The UDP moiety binds in a pocket in the C-Cat domain near the interface with the N-Cat domain. This pocket is lined with conserved residues shown to be important for catalytic activity. A transitional helix links the catalytic region to the

tetratricopeptide repeat (TPR), which caps the top of the catalytic region. The TPRs and the catalytic region are demarcated by a narrow horizontal cleft. Upon opening of the cleft due to a hinge-like movement of certain TPR units away from the catalytic domain the substrate enters the active site through the cleft between the catalytic region and the TPR domain, with the TPR domain regulating access. Since the TPR units have considerable flexibility relative to one

23

another, the cleft may open wider to accommodate larger protein substrates. Substrate peptides may bind in the cleft between the TPR domain and the catalytic region, at the interface between the N-Cat and C-Cat domains serines and/or threonine residues may be glycosylated by OGT. The side chain of the target serine or threonine may point directly into the nucleotide- sugar binding site near the location of the anomeric carbon of the GlcNAc sugar. The two residues N- terminal to the reactive target serine or threonine may lie directly over the UDP moiety; the residues C-terminal may traverse towards the back of the cleft along the long N-terminal helix that forms the top of the N-Cat domain. The C-Cat, N-Cat, UDP moiety, peptide substrate interface (pocket, cleft, entrance), and the catalytic core are depicted in Figures la-c, 2a-c, 2e, 6 and 7. The core of the OGT active site includes residues H498 and K842. The active site of OGT, the peptide substrate binding site, and the binding site of the UDP moiety further comprise D431, N458, H499, D523, H558, T560, R637, L653, Q839, K842, K898, H901, H920, T921, and D925. The three-dimensional structure of the active site of human OGT is provided by the atomic coordinates listed in Tables 5 (binary complex of OGT and UDP), Table 6 (ternary complex of OGT, UDP, and peptide substrate), and Table 7 (ternary complex of OGT, UDP, and glycopeptide).

[0027] Amino acid residues in proteins or peptides are abbreviated as follows:

phenylalanine is Phe or F; leucine is Leu or L; isoleucine is He or I; methionine is Met or M; valine is Val or V; serine is Ser or S; proline is Pro or P; threonine is Thr or T; alanine is Ala or A; tyrosine is Tyr or Y; histidine is His or H; glutamine is Gin or Q; asparagine is Asn or N; lysine is Lys or K; aspartic acid is Asp or D; glutamic Acid is Glu or E; cysteine is Cys or C; tryptophan is Trp or W; arginine is Arg or R; and glycine is Gly or G. For further description of amino acids, see Proteins: Structure and Molecular Properties by Creighton T. E. (1983), W. H. Freeman & Co., New York, incorporated herein by reference.

[0028] The term "atomic coordinates" refers to mathematical coordinates derived from mathematical equations related to the patterns obtained on diffraction of a monochromatic beam of x-rays by the atoms (scattering centers) of a protein molecule in crystal form. The diffraction data are used to calculate an electron density map of the repeating unit of the crystal. The electron density map is then used to establish the positions of the individual atoms within the unit cell of the crystal. The coordinates can also be obtained by means of computational analysis.

[0029] As used herein, a "binding compound" refers to a compound which reversibly or irreversibly binds to OGT. In certain embodiments, the binding compound binds in the active site of OGT. A binding compound may be an inhibitor of OGT (i.e., eliciting inhibition or reduction in enzymatic activity) or an activator of OGT (i.e., eliciting an increase in enzymatic activity). In certain embodiments, inhibitor compounds can, for example, be substrate analogs. Examples of OGT peptide substrates are provided in Table 4. These peptide substrates may be modified, for example by changing serine and/or threonine residues to an amino acid lacking a hydroxyl group in the side chain (e.g., alanine), introducing non-natural amino acids or chemical moieties that are linked to one or more of the amino acids of the peptide substrate. These chemical moieties may change the characteristics of the peptide, e.g., its charge, hydrophilicity/hydrophobicity, sterical distribution (spatial arrangement), and/or secondary structure so that the peptide may bind but not be processed by OGT, that is O-GlcNAcylation of the peptide may be inhibited. In certain embodiments, inhibitor compounds can, for example, be small molecules, such as UDP or a UDP-GlcNAc variant that may fit into the UDP-GlcNAc binding site but cannot be processed by OGT into UDP and GlcNAc. In other embodiments, small molecule inhibitors may be compounds that include a quinolinone or dihdyroquinolinone core as described in U.S. Patent Application, U.S.S.N.: 61/217,514, filed June 01, 2009, and International Application No.

PCT/US2010/001596, filed June 01, 2010, which are incorporated herein by reference. In other embodiments, small molecule inhibitors may be compounds described in U.S. Patent

Application, U.S.S.N.: 61/504,958, filed July 06, 2011. In certain embodiments, the small molecule inhibitors have a s

[0030] "Proliferative disease" as used herein refers to an uncontrolled growth of cells which interferes with the normal functioning of the bodily organs and systems. One form of proliferative disease is cancer. Cancers, such as invasive cancers, may migrate from their original location and seed vital organs and can eventually lead to the death of the subject through the functional deterioration of the affected organs. Carcinomas are malignant cancers that arise from epithelial cells and include adenocarcinoma and squamous cell carcinoma. Sarcomas are cancer of the connective or supportive tissue and include osteosarcoma, chondrosarcoma and gastrointestinal stromal tumor. Hematopoietic cancers, such as leukemia, are able to outcompete the normal hematopoietic compartments in a subject, thereby leading to hematopoietic failure (in the form of anemia, thrombocytopenia and neutropenia) ultimately causing death. A person of ordinary skill in the art can classify a cancer as a sarcoma, carcinoma or hematopoietic cancer.

[0031] By "choosing" is meant picking a chemical compound from a chemical library or commercially available source.

[0032] By "design" or "designing" is meant to provide a novel molecular structure of, for example, a compound, such as a small molecule, or a polypeptide or nucleic acid that has desired properties or characteristics.

[0033] The term "diabetic" as used herein, means a subject who, at the time the sample is taken, has a primary deficiency of insulin. The term diabetic includes, but is not limited to, individuals with juvenile diabetes (Type 1 diabetes), adult-onset diabetes (Type 2 diabetes), gestational diabetes, and any other conditions of insulin deficiency. The terms "diabetic" and "diabetes" are terms of art, known and understood by those practicing in the medical profession, a formal definition of which can be found in Harrison 's Principles of Medicine (Harrisons, Vol 14, Principles of Internal Medicine, Eds. Fauci, A.S., E. Braunwald, K.J. Isselbacher, J.D.

Wilson, J.B. Martin, D.L. Kasper, S.L. Hauser, D.L. Longo, McGraw-Hill, New York, 1999). As used herein, the term "complication of diabetes" is used to mean a condition that is associated with diabetes. Non-limiting examples of complications of diabetes include, but are not limited to, microvascular damage, insulin resistance, vascular damage, nephropathy, skin ulcers, circulatory damage, diabetic nephropathy, diabetic retinopathy, macro-vascular disease, microvascular disease, cardiac dysfunction, and diabetic neuropathy. Subjects with blood glucose levels that are higher than normal but not yet in the range associated with a diagnosis of diabetes may be considered to have "pre-diabetes." Pre-diabetes is also known in the art as "impaired fasting glucose" (IFG) or "impaired glucose tolerance" (IGT). Subjects with pre-diabetes have a higher risk of developing type 2 diabetes, which is also known as adult-onset diabetes or noninsulin-dependent diabetes. "Insulin resistance," as used herein, is a condition in which the tissues of the body fail to respond normally to insulin. DeFronzo, R. A. /. Cardiomuscular Pharmacology 20 (Suppl. 11): S1-S16 (1992). Insulin resistance manifests itself in

pathologically elevated endogenous insulin and glucose levels and predisposes one who suffers from said resistance to the development of a cluster of abnormalities, including some degree of impaired glucose tolerance, an increase in plasma triglycerides and low density lipoprotein cholesterol (LDL) levels, a decrease in high-density lipoprotein cholesterol (HDL) levels, high blood pressure, hyperuricemia, a decrease in plasma fibrinolytic activity, and/or an increase in cardiovascular disease and atherosclerosis. Reaven, G. M. Physiol-Rev. 75(3): 473-86 (1995).

[0034] The terms "effective amount" and "therapeutically effective amount," as used herein, refer to the amount or concentration of an inventive compound, that, when administered to a subject, is effective to at least partially treat a condition from which the subject is suffering.

[0035] By "identify" or "identifying" is meant to determine a condition, compound, polypeptide, amino acid, or nucleic acid that corresponds to or exhibits a desired characteristic or property.

[0036] As used herein the term "inhibit" means to reduce the amount of OGT activity and/or O-GlcNAcylation to a level or amount that is statistically significantly less than an initial level, which may be a baseline level of OGT activity and/or O-GlcNAcylation.

[0037] The term "modulate," as used herein, means to increase or decrease OGT enzymatic activity.

[0038] As used herein O-GlcNAc transferase "OGT" refers to not only human native

(natural occurring) or wild-type O-GlcNAc transferase (SEQ ID NO.: 53), but also includes any isoforms, variants, homologs, orthologs or modifications thereof. OGT homologs and orthologs include OGT from bacteria (e.g., Xanthomonas campestris as described in Clarke et al. EMBO J. 2008; 27(20):2780ff.) and mammalian homologs (e.g., mouse, rat, hamster, pig, goat, cow, camel, sheep, cat, dog), zebrafish, and plant (Arabidopsis thaliana). The OGT gene is capable of producing three separate transcripts, each of which encodes a different OGT isoform. The longest isoform, nucleocytoplasmic OGT (ncOGT) is encoded by all 23 exons, produces a protein of 116 kDa and is localized to both the nucleus and cytoplasm (Hanover et al., Arch. Biochem. Biophys., 409(2), 287-297, 2003). The second longest isoform, mitochondrial OGT (mOGT) is encoded by exons 5-23 and produces a protein of 103 kDa, contains a mitochondrial targeting sequence at its N-terminus and is localized to mitochondria (Love et al., J. Cell Set, 116(4), 647-654, 2003). The shortest isoform, short OGT (sOGT) is encoded by exons 10-23, produces a protein of 78 kDa, is ubiquitously expressed within the cell and is localized to both the nucleus and the cytoplasm (Nolte and Muller, Mamm. Genome, 13(1), 62-64, 2002; Hanover et al., Arch. Biochem. Biophys., 409(2), 287-297, 2003). Structural modifications include any additions, deletions, and/or substitutions to the native OGT amino acid sequence, post- translational modifications (e.g., phosphorylation, glycosylation, ubiquitination, etc.), and/or coordinating solvates, hydrates, or non-covalently bound ligands/substrates (e.g., UDP-GlcNAc, UDP, and/or a peptide substrate, such as the peptide substrates set forth in Table 4). Such structurally modified OGT are referred herein also as "OGT variant" or "OGT variants." A "variant" of OGT may also be a polypeptide which contains one or more modifications to the primary amino acid sequence of a naturally occurring OGT polypeptide. Structurally modified OGT or variant OGT include OGT that comprise one or more amino acid additions, deletions, and/or substitutions that are associated with disease. Such structurally modified OGT are referred herein also as "OGT mutant(s)" or "mutant OGT." In certain embodiments, variant or mutant OGT may have altered function relative to the polypeptide of the unmodified (naturally occurring) or wild-type amino acid sequence. For example, active site residues (H498), UDP- GlcNAc coordinating residues (R904, A896 (backbone), H901, K898, Q839, T922, K842, H920 (backbone) T921, T560 (backbone), L653 (backbone)) and/or peptide substrate binding residues (K634 (backbone), H496, H558) may be altered. Examples of such mutants are provided in Table 3. Other structurally modified OGTs include OGT isoforms. For example, three human isoforms of OGT are known, sOGT, mOGT, and ncOGT (depicted in Figure la), which differ in the number of TPR repeats. Other structurally modified OGTs include members of the OGT family, such as OGT homologs or orthologs from the same or different species. Known OGT homologs or orthologs include OGT from bacteria (e.g., Xanthomonas campestris as described in Clarke et ah, EMBO J. 2008; 27(20):2780ff.) and mammalian homologs (e.g. mouse and rat), zebrafish, plant (Arabidopsis thaliana) and Drosophila melanogaster (Gambetta et al. , Science, 2009; 325(5936):93-96). OGT has been cloned, for example, from humans, mouse, rat,

Caenorhabditis elegans, Drosophila melanogaster, and Arabidopsis thaliana, encoding all three isoforms (Nolte and Muller, Mamm. Genome, 13(1), 62-64, 2002; Hanover et al., Arch.

Biochem. Biophys., 409(2), 287-297, 2003), that is short OGT (sOGT), mitochondrial OGT (mOGT), and nucleocytoplasmic OGT (ncOGT) (also depicted in Figure 1A). Drosophila melanogaster and C. elegans is believed to contain one gene that is predicted to encode the ncOGT isoform (Hanover et al., Proc. Natl. Acad. Sci. U. S. A., 102(32), 11266-11271, 2005), whereas A. thaliana is believed to contain two separate genes that have been shown to have OGT activity (Hartweck et al., Genetics, 161(3), 1279-1291, 2002; Chen et al., J. Virol., 79(15), 9381-9387, 2005). In certain embodiments, OGT refers to a mammalian OGT. In certain embodiments, OGT refers to human OGT.

[0039] As used herein, the terms "O-GlcNAcylation-associated disease or disorder" and

"OGT- associated disease or disorder" include, but are not limited to diseases and disorders in which there is abnormal OGT activity and/or abnormal levels of O-GlcNAcylation. As used herein, the term "OGT activity" means OGT-mediated O-GlcNAcylation. An abnormal level of OGT activity and/or O-GlcNAcylation may be a level that is higher than a normal level or may be a level that is lower than a normal level, wherein a "normal" level is the level in a subject who does not have a disease or disorder associated with OGT activity or O-GlcNAcylation.

Examples of diseases and disorders associated with OGT activity and/or O-GlcNAcylation levels include, but are not limited to, neurodegenerative disorders such as Alzheimer's disease;

proliferative diseases (e.g., cancer); diabetes mellitus, insulin resistance, and complications of diabetes or other OGT- associated diseases.

[0040] By "screen" or "screening" is meant to test for in silico, in vitro, or in vivo a compound with a particular characteristic or desired property. These characteristics or desired properties may be chemical, biological, or physical in nature or a combination thereof. For example, in screening for OGT binding compounds the desired characteristics may include, but are not limited to, high affinity intracellular binding to OGT, low affinity intracellular binding to OGT, high specificity for binding to one or multiple binding sites on OGT, low specificity for binding to one or multiple binding sites on OGT, high degree of inhibition of OGT activity, high bioavailability of the compound, efficient cellular uptake of the compound, high solubility of the compound in pharmacological carriers, low pharmacological toxicity of the compound, etc. Screening may be performed in vitro or in vivo using compound libraries, such as small molecule libraries, peptide libraries, DNA libraries, of RNA. Screening in silico may be performed using predefined or randomized screening parameters and data sets, for example, of known test compounds and/or test conditions.

[0041] By "select" or "selecting" is meant to provide a pre-existing molecular structure and to chose, for example, from a group of pre-existing compounds, such as a small molecules, polypeptides or nucleic acids one or more members that have or exhibit a desired property or characteristic. [0042] The term "small molecule" as used herein is meant to describe a low molecular weight non-peptidic, non-oligomeric organic compound either synthesized in the laboratory or found in nature. A small molecule is typically characterized in that it contains several carbon- carbon bonds, and has a molecular weight of less than 1500 Da, although this characterization is not intended to be limiting for the purposes of the present invention. Small molecules may be smaller than about 1000 Da, smaller than about 800 Da, or smaller than about 500 Da. A small molecule may bind with high or low affinity to a biopolymer such as protein (e.g., OGT), nucleic acid, or polysaccharide and may in addition alter the activity or function of the biopolymer.

[0043] The term "space group" refers to the arrangement of symmetry elements in a crystal.

[0044] By "substrate" is meant a compound that acted upon by OGT, such as e.g. UDP-

GlcNAc and/or a peptide substrate, for example any one of the peptide substrates set forth in Table 4.

[0045] The term "subject," as used herein, refers to any animal. In certain embodiments, the subject is a mammal. In certain embodiments, the term "subject", as used herein, refers to a human (e.g., male, female, adult, or child). The subject may be at any stage of development. The subject may be a transgenic animal and/or experimental animal, e.g. a mammal (mouse, rat, hamster, pig, goat, cow, camel, sheep, cat, dog, etc.), a fish (zebrafish etc.), a nematode

(Caenorhabditis elegans etc.), an insect (Drosophila melanogaster etc.), a frog (Xenopus laevis).

[0046] By the term "synthesizing" is meant making a chemical structure from precursors by chemical processes. Synthesizing implies making at least one compound, but is not limited to one compound. In certain aspects, synthesizing implies making more than one compound, such as a series of compounds synthesized in an effort to study structure-activity relationships (SAR) using standard chemistry methods, and/or a series of structurally similar compounds made using standard combinatorial techniques.

[0047] As used herein, the terms "treatment," "treat," and "treating" refer to reversing, alleviating, delaying the onset of, or inhibiting the progress of a disease or disorder, or one or more symptoms thereof, as described herein. In some embodiments, treatment may be administered after one or more symptoms have developed. In other embodiments, treatment may be administered in the absence of symptoms. For example, treatment may be administered to a susceptible individual prior to the onset of symptoms (e.g., in light of a history of symptoms and/or in light of genetic or other susceptibility factors). Treatment may also be continued after symptoms have resolved, for example, to prevent or delay their recurrence.

[0048] The term "unit cell" refers to the basic parallelipiped shaped block. The entire volume of a crystal may be constructed by regular assembly of such blocks.

[0049] It will be appreciated that compounds that modulate OGT activity, such as, for example, inhibitors of OGT activity, may be small molecules. These small molecules may have chemical structures that can be altered. For example, one or more substituents of identified compounds may be substituted with any number of other substituents or functional moieties. When more than one position in any given structure may be substituted with more than one substituent selected from a specified group, the substituent may be either the same or different at every position. As used herein, the term "substituted" is contemplated to include substitution with all permissible substituents of organic compounds, any of the substituents described herein (for example, aliphatic, alkyl, alkenyl, alkynyl, heteroaliphatic, heterocyclic, aryl, heteroaryl, acyl, oxo, imino, thiooxo, cyano, isocyano, amino, azido, nitro, hydroxyl, thiol, halo, etc.), and any combination thereof (for example, aliphaticamino, heteroaliphaticamino, alkylamino, heteroalkylamino, arylamino, heteroarylamino, alkylaryl, arylalkyl, aliphaticoxy,

heteroaliphaticoxy, alkyloxy, heteroalkyloxy, aryloxy, heteroaryloxy, aliphaticthioxy, heteroaliphaticthioxy, alkylthioxy, heteroalkylthioxy, arylthioxy, heteroarylthioxy, acyloxy, and the like) that results in the formation of a stable moiety. Heteroatoms such as nitrogen may have hydrogen substituents and/or any suitable substituent as described herein which satisfy the valencies of the heteroatoms and results in the formation of a stable moiety.

[0050] As used herein, substituent names which end in the suffix "-ene" refer to a biradical derived from the removal of two hydrogen atoms from the substitutent. Thus, for example, acyl is acylene; alkyl is alkylene; alkeneyl is alkenylene; alkynyl is alkynylene;

heteroalkyl is heteroalkylene, heteroalkenyl is heteroalkenylene, heteroalkynyl is

heteroalkynylene, aryl is arylene, and heteroaryl is heteroarylene.

[0051] The term "acyl," as used herein, refers to a group having the general formula -

C(=0)Rxl, -C(=0)ORxl, -C(=0)-0-C(=0)Rxl, -C(=0)SRxl, -C(=0)N(Rxl)2, -C(=S)RX1, - C(=S)N(RX1)2, and -C(=S)S(RX1), -C(=NRX1)RX1, -C(=NRxl)ORxl, -C(=NRX1)SRX1, and -

XI XI XI

C(=NR )N(R )2, wherein R is hydrogen; halogen; substituted or unsubstituted hydroxyl; substituted or unsubstituted thiol; substituted or unsubstituted amino; substituted or unsubstituted acyl, cyclic or acyclic, substituted or unsubstituted, branched or unbranched aliphatic; cyclic or acyclic, substituted or unsubstituted, branched or unbranched hetero aliphatic; cyclic or acyclic, substituted or unsubstituted, branched or unbranched alkyl; cyclic or acyclic, substituted or unsubstituted, branched or unbranched alkenyl; substituted or unsubstituted alkynyl; substituted or unsubstituted aryl, substituted or unsubstituted heteroaryl, aliphaticoxy, heteroaliphaticoxy, alkyloxy, heteroalkyloxy, aryloxy, heteroaryloxy, aliphaticthioxy, heteroaliphaticthioxy, alkylthioxy, heteroalkylthioxy, arylthioxy, hetero arylthioxy, mono- or di- aliphaticamino, mono- or di- heteroaliphaticamino, mono- or di- alkylamino, mono- or di- heteroalkylamino,

XI

mono- or di- arylamino, or mono- or di- heteroarylamino; or two R groups taken together form a 5- to 6- membered heterocyclic ring. Exemplary acyl groups include aldehydes (-CHO), carboxylic acids (-C02H), ketones, acyl halides, esters, amides, imines, carbonates, carbamates, and ureas. Acyl substituents include, but are not limited to, any of the substituents described herein, that result in the formation of a stable moiety (e.g. , aliphatic, alkyl, alkenyl, alkynyl, heteroaliphatic, heterocyclic, aryl, heteroaryl, acyl, oxo, imino, thiooxo, cyano, isocyano, amino, azido, nitro, hydroxyl, thiol, halo, aliphaticamino, heteroaliphaticamino, alkylamino,

heteroalkylamino, arylamino, heteroarylamino, alkylaryl, arylalkyl, aliphaticoxy,

heteroaliphaticoxy, alkyloxy, heteroalkyloxy, aryloxy, heteroaryloxy, aliphaticthioxy, heteroaliphaticthioxy, alkylthioxy, heteroalkylthioxy, arylthioxy, heteroarylthioxy, acyloxy, and the like, each of which may or may not be further substituted).

[0052] The term "acyloxy" refers to a "substituted hydroxyl" of the formula (-OR1), wherein R1 is an optionally substituted acyl group, as defined herein, and the oxygen moiety is directly attached to the parent molecule.

[0053] The term "aliphatic," as used herein, includes both saturated and unsaturated, straight chain (i.e., unbranched), branched, acyclic, and cyclic (i.e. , carbocyclic) hydrocarbons, which are optionally substituted with one or more functional groups. As will be appreciated by one of ordinary skill in the art, "aliphatic" is intended herein to include, but is not limited to, alkyl, alkenyl, alkynyl, cycloalkyl, cycloalkenyl, and cycloalkynyl moieties. Thus, as used herein, the term "alkyl" includes straight, branched and cyclic alkyl groups. An analogous convention applies to other generic terms such as "alkenyl", "alkynyl", and the like.

Furthermore, as used herein, the terms "alkyl", "alkenyl", "alkynyl", and the like encompass both substituted and unsubstituted groups. In certain embodiments, as used herein, "aliphatic" is used to indicate those aliphatic groups (cyclic, acyclic, substituted, unsubstituted, branched or unbranched) having 1-20 carbon atoms. Aliphatic group substituents include, but are not limited to, any of the substituents described herein, that result in the formation of a stable moiety (e.g., aliphatic, alkyl, alkenyl, alkynyl, heteroaliphatic, heterocyclic, aryl, heteroaryl, acyl, oxo, imino, thiooxo, cyano, isocyano, amino, azido, nitro, hydroxyl, thiol, halo, aliphaticamino,

heteroaliphaticamino, alkylamino, heteroalkylamino, arylamino, heteroarylamino, alkylaryl, arylalkyl, aliphaticoxy, heteroaliphaticoxy, alkyloxy, heteroalkyloxy, aryloxy, heteroaryloxy, aliphaticthioxy, heteroaliphaticthioxy, alkylthioxy, heteroalkylthioxy, arylthioxy,

heteroarylthioxy, acyloxy, and the like, each of which may or may not be further substituted).

[0054] The term "alkyl," as used herein, refers to saturated, straight- or branched-chain hydrocarbon radicals derived from a hydrocarbon moiety containing between one and twenty carbon atoms by removal of a single hydrogen atom. In some embodiments, the alkyl group employed in the invention contains 1-20 carbon atoms. In another embodiment, the alkyl group employed contains 1-15 carbon atoms. In another embodiment, the alkyl group employed contains 1-10 carbon atoms. In another embodiment, the alkyl group employed contains 1-8 carbon atoms. In another embodiment, the alkyl group employed contains 1-5 carbon atoms. Examples of alkyl radicals include, but are not limited to, methyl, ethyl, n-propyl, isopropyl, n- butyl, iso-butyl, sec-butyl, sec-pentyl, iso-pentyl, tert-butyl, n-pentyl, neopentyl, n-hexyl, sec- hexyl, n-heptyl, n-octyl, n-decyl, n-undecyl, dodecyl, and the like, which may bear one or more sustitutents. Alkyl group substituents include, but are not limited to, any of the substituents described herein, that result in the formation of a stable moiety (e.g. , aliphatic, alkyl, alkenyl, alkynyl, heteroaliphatic, heterocyclic, aryl, heteroaryl, acyl, oxo, imino, thiooxo, cyano, isocyano, amino, azido, nitro, hydroxyl, thiol, halo, aliphaticamino, heteroaliphaticamino, alkylamino, heteroalkylamino, arylamino, heteroarylamino, alkylaryl, arylalkyl, aliphaticoxy, heteroaliphaticoxy, alkyloxy, heteroalkyloxy, aryloxy, heteroaryloxy, aliphaticthioxy, heteroaliphaticthioxy, alkylthioxy, heteroalkylthioxy, arylthioxy, heteroarylthioxy, acyloxy, and the like, each of which may or may not be further substituted).

[0055] The term "alkenyl," as used herein, denotes a monovalent group derived from a straight- or branched-chain hydrocarbon moiety having at least one carbon-carbon double bond by the removal of a single hydrogen atom. In certain embodiments, the alkenyl group employed in the invention contains 2-20 carbon atoms. In some embodiments, the alkenyl group employed in the invention contains 2-15 carbon atoms. In another embodiment, the alkenyl group employed contains 2-10 carbon atoms. In still other embodiments, the alkenyl group contains 2- 8 carbon atoms. In yet other embodiments, the alkenyl group contains 2-5 carbons. Alkenyl groups include, for example, ethenyl, propenyl, butenyl, l-methyl-2-buten-l-yl, and the like, which may bear one or more substituents. Alkenyl group substituents include, but are not limited to, any of the substituents described herein, that result in the formation of a stable moiety (e.g., aliphatic, alkyl, alkenyl, alkynyl, heteroaliphatic, heterocyclic, aryl, heteroaryl, acyl, oxo, imino, thiooxo, cyano, isocyano, amino, azido, nitro, hydroxyl, thiol, halo, aliphaticamino, heteroaliphaticamino, alkylamino, heteroalkylamino, arylamino, heteroarylamino, alkylaryl, arylalkyl, aliphaticoxy, heteroaliphaticoxy, alkyloxy, heteroalkyloxy, aryloxy, heteroaryloxy, aliphaticthioxy, heteroaliphaticthioxy, alkylthioxy, heteroalkylthioxy, arylthioxy,

heteroarylthioxy, acyloxy, and the like, each of which may or may not be further substituted).

[0056] The term "alkynyl," as used herein, refers to a monovalent group derived from a straight- or branched-chain hydrocarbon having at least one carbon-carbon triple bond by the removal of a single hydrogen atom. In certain embodiments, the alkynyl group employed in the invention contains 2-20 carbon atoms. In some embodiments, the alkynyl group employed in the invention contains 2-15 carbon atoms. In another embodiment, the alkynyl group employed contains 2-10 carbon atoms. In still other embodiments, the alkynyl group contains 2-8 carbon atoms. In still other embodiments, the alkynyl group contains 2-5 carbon atoms. Representative alkynyl groups include, but are not limited to, ethynyl, 2-propynyl (propargyl), 1-propynyl, and the like, which may bear one or more substituents. Alkynyl group substituents include, but are not limited to, any of the substituents described herein, that result in the formation of a stable moiety (e.g., aliphatic, alkyl, alkenyl, alkynyl, heteroaliphatic, heterocyclic, aryl, heteroaryl, acyl, oxo, imino, thiooxo, cyano, isocyano, amino, azido, nitro, hydroxyl, thiol, halo,

aliphaticamino, heteroaliphaticamino, alkylamino, heteroalkylamino, arylamino,

heteroarylamino, alkylaryl, arylalkyl, aliphaticoxy, heteroaliphaticoxy, alkyloxy, heteroalkyloxy, aryloxy, heteroaryloxy, aliphaticthioxy, heteroaliphaticthioxy, alkylthioxy, heteroalkylthioxy, arylthioxy, heteroarylthioxy, acyloxy, and the like, each of which may or may not be further substituted).

[0057] The term "amino," as used herein, refers to a group of the formula (-NH2). A

"substituted amino" refers either to a mono-substituted amine (-NHRh) of a disubstitued amine (-NRh 2), wherein the Rh substituent is any substitutent as described herein that results in the formation of a stable moiety (e.g., a suitable amino protecting group; aliphatic, alkyl, alkenyl, alkynyl, heteroaliphatic, heterocyclic, aryl, heteroaryl, acyl, amino, nitro, hydroxyl, thiol, halo, aliphaticamino, heteroaliphaticamino, alkylamino, heteroalkylamino, arylamino,

heteroarylamino, alkylaryl, arylalkyl, aliphaticoxy, heteroaliphaticoxy, alkyloxy, heteroalkyloxy, aryloxy, heteroaryloxy, aliphaticthioxy, heteroaliphaticthioxy, alkylthioxy, heteroalkylthioxy, arylthioxy, heteroarylthioxy, acyloxy, and the like, each of which may or may not be further substituted). In certain embodiments, the Rh substituents of the di-substituted amino group(- NRh 2) form a 5- to 6- membered hetereocyclic ring.

[0058] The term "alkoxy" refers to a "substituted hydroxyl" of the formula (-OR1), wherein R1 is an optionally substituted alkyl group, as defined herein, and the oxygen moiety is directly attached to the parent molecule.

[0059] The term "alkylthioxy" refers to a "substituted thiol" of the formula (-SRr), wherein Rr is an optionally substituted alkyl group, as defined herein, and the sulfur moiety is directly attached to the parent molecule.

[0060] The term "alkylamino" refers to a "substituted amino' Of the formula (-NRh 2), wherein Rh is, independently, a hydrogen or an optionally subsituted alkyl group, as defined herein, and the nitrogen moiety is directly attached to the parent molecule.

[0061] The term "aryl," as used herein, refer to stable aromatic mono- or polycyclic ring system having 3-20 ring atoms, of which all the ring atoms are carbon, and which may be substituted or unsubstituted. In certain embodiments of the present invention, "aryl" refers to a mono, bi, or tricyclic C4-C2o aromatic ring system having one, two, or three aromatic rings which include, but not limited to, phenyl, biphenyl, naphthyl, and the like, which may bear one or more substituents. Aryl substituents include, but are not limited to, any of the substituents described herein, that result in the formation of a stable moiety (e.g. , aliphatic, alkyl, alkenyl, alkynyl, heteroaliphatic, heterocyclic, aryl, heteroaryl, acyl, oxo, imino, thiooxo, cyano, isocyano, amino, azido, nitro, hydroxyl, thiol, halo, aliphaticamino, heteroaliphaticamino, alkylamino, heteroalkylamino, arylamino, heteroarylamino, alkylaryl, arylalkyl, aliphaticoxy, heteroaliphaticoxy, alkyloxy, heteroalkyloxy, aryloxy, heteroaryloxy, aliphaticthioxy, heteroaliphaticthioxy, alkylthioxy, heteroalkylthioxy, arylthioxy, heteroarylthioxy, acyloxy, and the like, each of which may or may not be further substituted). [0062] The term "arylalkyl," as used herein, refers to an aryl substituted alkyl group, wherein the terms "aryl" and "alkyl" are defined herein, and wherein the aryl group is attached to the alkyl group, which in turn is attached to the parent molecule. An exemplary arylalkyl group includes benzyl.

[0063] The term "aryloxy" refers to a "substituted hydroxyl" of the formula (-OR1), wherein R1 is an optionally substituted aryl group, as defined herein, and the oxygen moiety is directly attached to the parent molecule.

[0064] The term "arylamino," refers to a "substituted amino' Of the formula (-NRh 2), wherein Rh is, independently, a hydrogen or an optionally substituted aryl group, as defined herein, and the nitrogen moiety is directly attached to the parent molecule.

[0065] The term "arylthioxy" refers to a "substituted thiol" of the formula (-SRr), wherein Rr is an optionally substituted aryl group, as defined herein, and the sulfur moiety is directly attached to the parent molecule.

[0066] The term "azido," as used herein, refers to a group of the formula (-N3).

[0067] The term "cyano," as used herein, refers to a group of the formula (-CN).

[0068] The terms "halo" and "halogen," as used herein, refer to an atom selected from fluorine (fluoro, -F), chlorine (chloro, -CI), bromine (bromo, -Br), and iodine (iodo, -I).

[0069] The term "heteroaliphatic," as used herein, refers to an aliphatic moiety, as defined herein, which includes both saturated and unsaturated, nonaromatic, straight chain (i.e. , unbranched), branched, acyclic, cyclic (i.e. , heterocyclic), or polycyclic hydrocarbons, which are optionally substituted with one or more functional groups, and that contain one or more oxygen, sulfur, nitrogen, phosphorus, or silicon atoms, e.g., in place of carbon atoms. In certain embodiments, heteroaliphatic moieties are substituted by independent replacement of one or more of the hydrogen atoms thereon with one or more substituents. As will be appreciated by one of ordinary skill in the art, "heteroaliphatic" is intended herein to include, but is not limited to, heteroalkyl, heteroalkenyl, heteroalkynyl, heterocycloalkyl, heterocycloalkenyl, and heterocycloalkynyl moieties. Thus, the term "heteroaliphatic" includes the terms "heteroalkyl," "heteroalkenyl", "heteroalkynyl", and the like. Furthermore, as used herein, the terms

"heteroalkyl", "heteroalkenyl", "heteroalkynyl", and the like encompass both substituted and unsubstituted groups. In certain embodiments, as used herein, "heteroaliphatic" is used to indicate those heteroaliphatic groups (cyclic, acyclic, substituted, unsubstituted, branched or unbranched) having 1-20 carbon atoms. Heteroaliphatic group substituents include, but are not limited to, any of the substituents described herein, that result in the formation of a stable moiety (e.g., aliphatic, alkyl, alkenyl, alkynyl, heteroaliphatic, heterocyclic, aryl, heteroaryl, acyl, sulfinyl, sulfonyl, oxo, imino, thiooxo, cyano, isocyano, amino, azido, nitro, hydroxyl, thiol, halo, aliphaticamino, heteroaliphaticamino, alkylamino, heteroalkylamino, arylamino, heteroarylamino, alkylaryl, arylalkyl, aliphaticoxy, heteroaliphaticoxy, alkyloxy, heteroalkyloxy, aryloxy, heteroaryloxy, aliphaticthioxy, heteroaliphaticthioxy, alkylthioxy, heteroalkylthioxy, arylthioxy, heteroarylthioxy, acyloxy, and the like, each of which may or may not be further substituted).

[0070] The term "heteroalkyl," as used herein, refers to an alkyl moiety, as defined herein, which contain one or more oxygen, sulfur, nitrogen, phosphorus, or silicon atoms, e.g., in place of carbon atoms.

[0071] The term "heteroalkenyl," as used herein, refers to an alkenyl moiety, as defined herein, which contain one or more oxygen, sulfur, nitrogen, phosphorus, or silicon atoms, e.g., in place of carbon atoms.

[0072] The term "heteroalkynyl," as used herein, refers to an alkynyl moiety, as defined herein, which contain one or more oxygen, sulfur, nitrogen, phosphorus, or silicon atoms, e.g., in place of carbon atoms.

[0073] The term "heteroalkylamino" refers to a "substituted amino" of the formula (-

NRh 2), wherein Rh is, independently, a hydrogen or an optionally substituted heteroalkyl group, as defined herein, and the nitrogen moiety is directly attached to the parent molecule.

[0074] The term "heteroalkyloxy" refers to a "substituted hydroxyl" of the formula (-

OR1), wherein R1 is an optionally substituted heteroalkyl group, as defined herein, and the oxygen moiety is directly attached to the parent molecule.

[0075] The term "heteroalkylthioxy" refers to a "substituted thiol" of the formula (-SRr), wherein Rr is an optionally substituted heteroalkyl group, as defined herein, and the sulfur moiety is directly attached to the parent molecule.

[0076] The term "heterocyclic," "heterocycles," or "heterocyclyl," as used herein, refers to a cyclic heteroaliphatic group. A heterocyclic group refers to a non-aromatic, partially unsaturated or fully saturated, 3- to 10-membered ring system, which includes single rings of 3 to 8 atoms in size, and bi- and tri-cyclic ring systems which may include aromatic five- or six- membered aryl or heteroaryl groups fused to a non-aromatic ring. These heterocyclic rings include those having from one to three heteroatoms independently selected from oxygen, sulfur, and nitrogen, in which the nitrogen and sulfur heteroatoms may optionally be oxidized and the nitrogen heteroatom may optionally be quaternized. In certain embodiments, the term

heterocylic refers to a non-aromatic 5-, 6-, or 7-membered ring or polycyclic group wherein at least one ring atom is a heteroatom selected from O, S, and N (wherein the nitrogen and sulfur heteroatoms may be optionally oxidized), and the remaining ring atoms are carbon, the radical being joined to the rest of the molecule via any of the ring atoms. Heterocycyl groups include, but are not limited to, a bi- or tri-cyclic group, comprising fused five, six, or seven-membered rings having between one and three heteroatoms independently selected from the oxygen, sulfur, and nitrogen, wherein (i) each 5-membered ring has 0 to 2 double bonds, each 6-membered ring has 0 to 2 double bonds, and each 7-membered ring has 0 to 3 double bonds, (ii) the nitrogen and sulfur heteroatoms may be optionally oxidized, (iii) the nitrogen heteroatom may optionally be quaternized, and (iv) any of the above heterocyclic rings may be fused to an aryl or heteroaryl ring. Exemplary heterocycles include azacyclopropanyl, azacyclobutanyl, 1,3-diazatidinyl, piperidinyl, piperazinyl, azocanyl, thiaranyl, thietanyl, tetrahydrothiophenyl, dithiolanyl, thiacyclohexanyl, oxiranyl, oxetanyl, tetrahydrofuranyl, tetrahydropuranyl, dioxanyl,

oxathiolanyl, morpholinyl, thioxanyl, tetrahydronaphthyl, and the like, which may bear one or more substituents. Substituents include, but are not limited to, any of the substituents described herein, that result in the formation of a stable moiety (e.g., aliphatic, alkyl, alkenyl, alkynyl, heteroaliphatic, heterocyclic, aryl, heteroaryl, acyl, sulfinyl, sulfonyl, oxo, imino, thiooxo, cyano, isocyano, amino, azido, nitro, hydroxyl, thiol, halo, aliphaticamino, heteroaliphaticamino, alkylamino, heteroalkylamino, arylamino, heteroarylamino, alkylaryl, arylalkyl, aliphaticoxy, heteroaliphaticoxy, alkyloxy, heteroalkyloxy, aryloxy, heteroaryloxy, aliphaticthioxy, heteroaliphaticthioxy, alkylthioxy, heteroalkylthioxy, arylthioxy, heteroarylthioxy, acyloxy, and the like, each of which may or may not be further substituted).

[0077] The term "heteroaryl," as used herein, refer to stable aromatic mono- or polycyclic ring system having 3-20 ring atoms, of which one ring atom is selected from S, O, and N; zero, one, or two ring atoms are additional heteroatoms independently selected from S, O, and N; and the remaining ring atoms are carbon, the radical being joined to the rest of the molecule via any of the ring atoms. Exemplary heteroaryls include, but are not limited to pyrrolyl, pyrazolyl, imidazolyl, pyridinyl, pyrimidinyl, pyrazinyl, pyridazinyl, triazinyl, tetrazinyl, pyyrolizinyl, indolyl, quinolinyl, isoquinolinyl, benzoimidazolyl, indazolyl, quinolinyl, isoquinolinyl, quinolizinyl, cinnolinyl, quinazolynyl, phthalazinyl, naphthridinyl, quinoxalinyl, thiophenyl, thianaphthenyl, furanyl, benzofuranyl, benzothiazolyl, thiazolynyl, isothiazolyl, thiadiazolynyl, oxazolyl, isoxazolyl, oxadiaziolyl, oxadiaziolyl, and the like, which may bear one or more substituents. Heteroaryl substituents include, but are not limited to, any of the substituents described herein, that result in the formation of a stable moiety (e.g. , aliphatic, alkyl, alkenyl, alkynyl, heteroaliphatic, heterocyclic, aryl, heteroaryl, acyl, sulfinyl, sulfonyl, oxo, imino, thiooxo, cyano, isocyano, amino, azido, nitro, hydroxyl, thiol, halo, aliphaticamino, heteroaliphaticamino, alkylamino, heteroalkylamino, arylamino, heteroarylamino, alkylaryl, arylalkyl, aliphaticoxy, heteroaliphaticoxy, alkyloxy, heteroalkyloxy, aryloxy, heteroaryloxy, aliphaticthioxy, heteroaliphaticthioxy, alkylthioxy, heteroalkylthioxy, arylthioxy,

heteroarylthioxy, acyloxy, and the like, each of which may or may not be further substituted).

[0078] The term "heteroarylene," as used herein, refers to a biradical derived from an heteroaryl group, as defined herein, by removal of two hydrogen atoms. Heteroarylene groups may be substituted or unsubstituted. Additionally, heteroarylene groups may be incorporated as a linker group into an alkylene, alkenylene, alkynylene, heteroalkylene, heteroalkenylene, or heteroalkynylene group, as defined herein. Heteroarylene group substituents include, but are not limited to, any of the substituents described herein, that result in the formation of a stable moiety (e.g., aliphatic, alkyl, alkenyl, alkynyl, heteroaliphatic, heterocyclic, aryl, heteroaryl, acyl, oxo, imino, thiooxo, cyano, isocyano, amino, azido, nitro, hydroxyl, thiol, halo, aliphaticamino, heteroaliphaticamino, alkylamino, heteroalkylamino, arylamino, heteroarylamino, alkylaryl, arylalkyl, aliphaticoxy, heteroaliphaticoxy, alkyloxy, heteroalkyloxy, aryloxy, heteroaryloxy, aliphaticthioxy, heteroaliphaticthioxy, alkylthioxy, heteroalkylthioxy, arylthioxy,

heteroarylthioxy, acyloxy, and the like, each of which may or may not be further substituted).

[0079] The term "heteroarylamino" refers to a "substituted amino' Of the (-NRh 2), wherein Rh is, independently, a hydrogen or an optionally substituted heteroaryl group, as defined herein, and the nitrogen moiety is directly attached to the parent molecule.

[0080] The term "heteroaryloxy" refers to a "substituted hydroxyl" of the formula (-

OR1), wherein R1 is an optionally substituted heteroaryl group, as defined herein, and the oxygen moiety is directly attached to the parent molecule. [0081] The term "heteroarylthioxy" refers to a "substituted thiol" of the formula (-SRr), wherein Rr is an optionally substituted heteroaryl group, as defined herein, and the sulfur moiety is directly attached to the parent molecule.

[0082] The term "hydroxy," or "hydroxyl," as used herein, refers to a group of the formula (-OH). A "substituted hydroxyl" refers to a group of the formula (-OR1), wherein R1 can be any substitutent which results in a stable moiety (e.g., a suitable hydroxyl protecting group; aliphatic, alkyl, alkenyl, alkynyl, heteroaliphatic, heterocyclic, aryl, heteroaryl, acyl, nitro, alkylaryl, arylalkyl, and the like, each of which may or may not be further substituted).

[0083] The term "imino," as used herein, refers to a group of the formula (=NRr), wherein Rr corresponds to hydrogen or any substitutent as described herein, that results in the formation of a stable moiety (for example, a suitable amino protecting group; aliphatic, alkyl, alkenyl, alkynyl, heteroaliphatic, heterocyclic, aryl, heteroaryl, acyl, amino, hydroxyl, alkylaryl, arylalkyl, and the like, each of which may or may not be further substituted). In certain embodiments, imino refers to =NH wherein Rr is hydrogen.

[0084] The term "isocyano," as used herein, refers to a group of the formula (-NC).

[0085] The term "nitro," as used herein, refers to a group of the formula (-N02).

[0086] The term "oxo," as used herein, refers to a group of the formula (=0).

BRIEF DESCRIPTION OF THE FIGURES

[0087] The patent or application file contains at least one drawing executed in color.

Copies of this patent or patent application publication with color drawings will be provided by the Office upon request and payment of the necessary fee.

[0088] Figure 1 depicts the overall structure of human OGT complexed to UDP. Figure la depicts a schematic of OGT domain architecture. The N-terminus consists of

tetratricopeptide repeat (TPR) units, shown in gray, each comprising a pair of a-helices. There are three isoforms of OGT— short OGT (sOGT), mitochondrial OGT (mOGT), and

nucleocytoplasmic OGT (ncOGT), which differ in the number of TPR repeats, as indicated. Provided herein is a crystallization construct, hOGT4 5, that contains 4.5 TPR units, as indicated. The TPRs are connected to the catalytic region by a transitional helix, shown in purple. The catalytic region comprises three domains, the N-terminal catalytic domain (N-Cat, shown in blue), the intervening domain (Int-D, shown in green), and the C-terminal catalytic domain (C- Cat, shown in red). Residue numbers demarcating the boundaries of key features are based on the numbering of full-length ncOGT. Figure lb depicts the overall fold of OGT from the OGT- UDP complex in a ribbon representation. The coloring is the same as the schematic in Figure la. UDP is shown in cyan. The additional helices in the N-Cat domain, which make OGT unique among GT-B superfamily members, are indicated as HI and H2. Figure lc is a surface representation of the OGT-UDP complex. The coloring scheme is the same as in Figures la and lb.

[0089] Figure 2 depicts the structure of the OGT-UDP-peptide complex. Figure 2a depicts a surface rendering of the OGT complex with UDP and the CKII peptide substrate (YPGGSTPVSSANMM, SEQ ID NO: 1). The view is the same as in Figure lc. The coloring scheme is the same as in Figure 1. The peptide is shown as a stick model with the carbons in yellow. UDP lies under the peptide in this view in a pocket in the C-Cat domain and is not visible. Figure 2b depicts a close-up surface view of the OGT active site looking down at the surface formed by the C-Cat and the N-Cat domains. The CKII peptide, with carbon atoms shown in yellow, binds in the cleft between the TPR region and the catalytic region along the interface between the C-Cat and N-Cat domains. The UDP moiety is shown as a surface rendering in purple directly beneath the N-terminal segment of the CKII peptide. The surface of OGT is shown in gray, with residues that have been implicated in catalytic activity colored orange, green, or blue in decreasing order of importance based on residual activity after mutation (provided in Table 3). Residue 842, colored orange, lies underneath UDP in this view. Figure 2c depicts a view of UDP (carbon atoms shown in cyan) and part of the CKII peptide substrate (carbon atoms shown in yellow) with selected OGT sidechains shown. Dashed lines indicate inferred hydrogen bonds based on distances of the structure. Electron density from an omit map is shown for UDP and the peptide at 1 sigma. Figure 2d depicts a histogram showing the relative activities of the H498A and H558A mutants compared to the wildtype protein (average + s.d., n=3). Figure 2e depicts the proposed mechanism of OGT. An ordered sequential kinetic mechanism in which UDP-GlcNAc binds first is depicted based on the structure of the ternary complex. A schematic of the reaction that takes place following sequential binding of both substrates is shown, with the peptide in yellow as a cartoon and only the reactive serine hydroxyl shown. The proposed catalytic base, His498, and the residue stabilizing the leaving group, Lys842, are indicated. [0090] Figure 3 depicts the structure and proposed function of the intervening domain.

Figure 3a, Ribbon representation of the intervening domain rendered in light green with loops for which there is no electron density represented by dotted lines. 12 residues are missing from one loop and five from the other. Also shown in coral is a helix from the C-cat domain that contains proposed PIP3 binding residues . Lysine sidechains that form an extensive positive surface (see Figure 3b) are displayed in "ball-and-stick" representation, with two residues mentioned in the text rendered in light blue. Figure 3b depicts a surface representation of OGT colored according to electrostatic potential. The protein is rotated 90 degrees around the X-axis from the representation shown in Figures 1, 2, and 3c, placing the bottom surface of the catalytic region in view. Blue represents areas of positive charge; red represents areas of negative charge; white is neutral. Figure 3c depicts a model of full-length OGT with the protein shown as a surface rendering and colored as in Figure la. The first two TPR units of hOGT4.5 overlap with the last two TPR units of the previously crystallized human TPR domain (PDB code 1W3B), (Jinek et ah, Nat Struct Mol Biol 11, 1001-7 (2004)) allowing the superimposition of these parts of the two structures and creation of a composite model of full length OGT (the extension of the TPR domain is colored in light grey). This model is shown as a monomer, although OGT may exist in different oligomerization states in cells (Jinek et ah, Nat Struct Mol Biol 11, 1001-7 (2004); Kreppel et al.L J Biol Chem 214, 32015-22 (1999)). Hinge and latch regions are indicated by arrows. Figure 3d depicts a model of full-length OGT opening to accommodate larger substrates. The "open" conformation shown is based on molecular dynamics simulations performed using the OGT-UDP-peptide structure (with UDP and the peptide removed) as a starting model.

[0091] Figure 4 depicts the kinetics of ncOGT and hOGT4 5 with the CKII3K peptide.

Figure 4a depicts a Eadie-Hofstee plot of ncOGT. This transformation of the kinetic data shows two distinct Kms for UDP-GlcNAc. The data were obtained under the following conditions: All assays were performed using 3 mM CKII3K peptide ((Kreppel et ah, J Biol Chem 274, 32015-22 (1999); Gross et ah, J Am Chem Soc 127, 14588-9 (2005)), while varying the concentration of UDP-14C-GlcNAc (300 mCi/mmol specific activity). Reactions were run for 30 min at room temperature with 32 nM of ncOGT and 40 nM of hOGT4 5 for the lower concentrations of UDP- GlcNAc and 600 nM enzyme for the higher Km measurements. Data were analyzed by

GraphPad Prism5. For greater accuracy, the Km values shown on the plots were determined by nonlinear regression analysis of the velocity versus substrate concentration curves (for an example Figure 4c). Figure 4b depicts a Eadie-Hofstee plot of hOGT4 5. Figure 4c depicts Michaelis-Menten curves for ncOGT and hOGT4 5 at saturating (3mM) CKII peptide concentrations and UDP-GlcNAc concentrations below 30 μΜ. Figure 4d depicts kinetic constants derived from the data shown in Figure 4c.

[0092] Figure 5 depicts product inhibition patterns by UDP supporting an ordered bi bi mechanism. Figure 5a depicts double reciprocal plot showing inhibition of ncOGT by UDP at saturating peptide concentrations (Graphpad Prism5; average + s.e.m., n=3). Reactions were performed in the presence of UDP at saturating peptide concentrations while varying UDP- GlcNAc levels (conditions: 80 nM purified ncOGT, 3.5 mM CKII3K peptide, UDP-GlcNAc varied from 0.625 to 30 μΜ, and UDP at the indicated, fixed concentrations; 30 minute incubation at room temperature). For a random bi bi mechanism at saturating peptide concentrations, no inhibition by UDP should be observed; for an ordered mechanism with UDP- GlcNAc binding first and UDP leaving last, UDP should be a competitive inhibitor with respect to UDP-GlcNAc under these conditions (Segel I.H. xxii, p.957, Wiley, New York, 1975;

Copeland R.A. xvi, p. 397, Wiley, New York, 2000). Linear regression analysis of the data is consistent with competitive inhibition (Vmax of -0.01 μΜ/min). Figure 5b depicts a double reciprocal plot showing inhibition of ncOGT by UDP at unsaturating UDP-GlcNAc conditions. Reactions were performed in the presence of UDP and unsaturating UDP-GlcNAc (1.2 μΜ) while varying peptide concentrations from 68 μΜ to 2.4 mM. Mixed inhibition, as observed, is expected for an ordered mechanism in which UDP-GlcNAc binds first, but it is not consistent with a rapid equilibrium random mechanism (Segel I.H. xxii, p.957, Wiley, New York, 1975; Copeland R.A. xvi, p. 397, Wiley, New York, 2000). For 0, 20, and 50 μΜ UDP, Vmax values of 0.01, 0.006, and 0.003 μΜ/min were calculated, respectively.

[0093] Figure 6 depicts the opening of the active site cleft. Superposition of the OGT-

UDP structure (yellow) and the OGT-UDP-peptide structure (gray) shows the movement of the TPRs upon substrate binding. The peptide (shown as a gray stick model) juts into TPR 12 (left arrow), which hinges open the cleft.

[0094] Figure 7 depicts the structure of UDP-GlcNAc docked into the active site. This fit is the highest ranking pose with a docking score of -12.785. The OGT-UDP structure was used to build energy grids using the default value of protein atom scaling (1.0) within a cubic box with sides of 24 A. The ligand and protein were parametrized with the OPLS2001 force field. Docking calculations were performed in Extra Precision mode. Generated ligand poses were scored by GlideScore (Schrodinger Software Suite. (Schrodinger LLC, New York, 2006)). Residues visible in this cut away view that make critical contacts with UDP-GlcNAc are indicated. The sidechain of His901 (not shown in the cutaway) also stacks directly over the uracil and we have confirmed its importance in catalytic activity via mutagenesis (provided in Table 3). The anomeric carbon of the GlcNAc residue is indicated by the yellow arrow. In this conformation, the β face of the sugar is exposed to the peptide, consistent with the proposed mechanism involving an SN2 displacement of UDP with inversion of configuration. A lower ranking pose in which the N-acetyl group points down into the pocket is sterically feasible and is consistent with the conformation observed in a complex of a bacterial OGT homolog bound to a UDP-GlcNAc C-glycoside analog (Clarke et al. Embo J 27, 2780-8 (2008)). However, the lower ranking pose is not consistent with the enzymatic reaction or with experimental evidence that the N-acetyl group of the GlcNAc is solvent exposed (Gross et al., J Am Chem Soc 127, 14588-9 (2005)).

[0095] Figure 8 depicts a sequence logo generated from proteins where the exact site of

O-GlcNAcylation is known. These peptides are listed in Table 4. The peptides were aligned such that the glycosylation site is in the middle at the "0" position, and the sequence was then truncated to include only four residues to the N-terminus of the glycosylation site ("-4") through four residues to the C-terminus of the site ("4"). The logo was generated using the online program "Protein Sequence Logos using Relative Entropy." (Gorodkin et al., Comput Appl Biosci 13, 583-6 (1997)), (Schneider et al, Nucleic Acids Res 18, 6097-100 (1990))

[0096] Figure 9 depicts the topology diagram of the intervening domain of OGT. 2 a- helices are represented by cylinders and β-strands are represented by arrows. Residue numbers are labeled. The three large loops of the domain are shown in blue.

[0097] Figure 10 depicts the relative activities of hOGT4.5 and hOGT4.5Aint. The intervening domain from the crystallization construct was replaced with a short peptide

(TSRVVAEPP, SEQ ID NO: 55) linking residues 697 to 821. The activity was measured using the CKII peptide filter-binding assay.

[0098] Figure 11 depicts the crystal packing interfaces. Figure 11a shows OGT-UDP crystal packing. OGT-UDP crystallized with four copies in the asymmetric unit in the P321 space group, but there is a threefold symmetry interface, as shown. This trimer may not be relevant for the full-length protein since it would not be able to form if there were more than 4.5 TPR units. Figure l ib shows OGT-UDP-CKII crystal packing. The OGT-UDP-CKII complex crystallized in the 1121 space group as a dimer, as shown. The several observed multimerization surfaces may not be physiologically relevant since equilibrium sedimentation ultracentrifugation experiments and gel filtration studies using the crystallization construct show that it is monomeric in solution.

DETAILED DESCRIPTION OF CERTAIN EMBODIMENTS OF THE INVENTION

[0099] The present invention is largely based on the x-ray crystal structures of human O-

GlcNAc transferase (OGT) provided herein. The present invention provides detailed three- dimensional structural information from single crystal X-ray crystallography of human OGT, for example, obtained from co-crystals of OGT as a binary complex with UDP (2.8 A) and of OGT as a ternary complex with UDP and a peptide substrate (1.95 A). Aberrant O-GlcNAcylation by OGT has been linked to, for example, insulin resistance,10 diabetic complications11, cancer12 and neurodegenerative diseases including Alzheimer's disease. 13 Despite the importance of OGT, the details of how the enzyme recognizes its protein substrates are largely unknown and the lack of a crystal structure of OGT has been a major impediment to developing inhibitors, to understanding substrate recognition, and to exploring OGT's molecular mechanisms. The atomic coordinates of human OGT provided herein and the structural information derived from the OGT models derived therefrom enable the rational (in silico) design of modulators of OGT activity including OGT inhibitors that may be useful in the treatment of human disease.

[00100] In one aspect, the invention provides screening methods for novel inhibitors of

OGT activity using the structural information of OGT provided herein. Compounds identified by the methods provided herein may be used to inhibit O-GlcNAc transferase (OGT) activity. OGT inhibitors identified by the methods described herein may be useful in the treatment of diseases associated with hyper-O-GlcNAcylation, such as for example, cancers,

neurodegenerative diseases, autoimmune diseases, and inflammatory diseases and may be formulated with a pharmaceutically acceptable excipient. Any binding compounds (such as inhibitors, activators, etc.) may be designed in silico based on the three-dimensional structural information provided by the atomic coordinates provided herein. Useful OGT binding compounds may, for example, be computationally identified using the atomic coordinates set forth in Tables 5, 6, or 7 to display the atomic coordinates as a three-dimensional structure of OGT with and without UDP or variants thereof, and with or without a peptide substrate (such as provided in Table 4) or variants thereof. OGT binding compounds may be identified that bind in the active site of OGT (e.g. the catalytic core, the binding site for UDP-GlcNAc or UDP, and/or the binding site for a peptide substrate) or to a site outside of the active site of OGT. The three- dimensional structural information provided by the atomic coordinates provided herein may also be used to model other OGTs, such as OGT isoforms, OGT mutants (synthetic or naturally occurring, examples are provided in Table 3), or OGT homologs or orthologs. OGT binding compounds may also be useful for other applications, such as scientific research, e.g., as stabilizing agents in crystallography (to provide co-crystals).

Cloning of OGT

[00101] The ogt gene may be cloned and the nucleic acid sequence of a wild-type ogt gene may be altered using standard protocols and techniques. "Altered ogt genes," include ogt genes encoding variant OGT polypeptides that comprise one or more mutations that, for example, change OGT's activity, such as the mutations provided in Table 3. Ogt gene expression vectors for recombinantly producing OGT can be any suitable expression vector, for example a modified pET24b vector (Novagen, Madison, WI) with a T7 tag and 8x His tag followed by an HRV3C protease cleavage site at the N-terminus. In certain embodiments, an ogt expression vector is provided that has a nucleic acid sequence set forth in SEQ ID NO: 3.

[00102] Nucleic acids for the production of recombinant proteins may be i) amplified in vitro by, for example, polymerase chain reaction (PCR); ii) recombinantly produced by cloning; iii) purified (e.g., from a sample or tissue), and isolated, for example, by gel separation; or iv) synthesized by, for example, chemical synthesis.

[00103] In certain embodiments, nucleic acids comprising a ogt gene or a portion thereof are provided. In certain embodiments, the nucleic acid comprise the sequence as set forth in SEQ ID NO: 3 or a portion thereof. In certain embodiments, a nucleic acid comprising a ogt gene variant is provided. In certain embodiments, the ogt gene variant comprises one or more nucleotide substitutions, additions, deletions, or duplications. In certain embodiments, a nucleic acid is provided that comprises an ogt gene variant encoding a mutation with decreased OGT activity, for example, a mutation as set forth in Table 3.

[00104] Modifications and mutations which create a OGT variant can be made within the nucleic acid sequence which encodes OGT. Modifications and mutations include deletions, point mutations, truncations, nucleic acid changes that lead to amino acid substitutions, and nucleic acid changes that lead to the addition of amino acids. OGT modifications that are introduced in vitro may resemble modifications that are naturally occurring or that decrease OGT enzymatic activity, e.g., mutations in the active site, and/or other mutations, such as provided in Table 3. Other modifications may include, for example, addition of a linker molecule, addition of a tag (e.g. T7 tag and/or poly His tag), addition of a detectable moiety, and addition of a cleavage site (e.g. HRV3C). Modifications also embrace fusion proteins comprising all or part of the amino acid sequence of OGT. The detailed three-dimensional structural information provided herein enable one of skill in the art to predict the effect on protein conformation of a change in protein sequence, and one can thus "design" a variant OGT polypeptide according to known methods.

[00105] Nucleic acid modifications can be made to generate variants that are silent with respect to the amino acid sequence of the encoded polypeptide, but which provide preferred codons for translation in a particular host. The preferred codons for translation of a nucleic acid in specific non-mammalian expression systems, such as prokaryotic systems, are well known in the art (e.g., Tats et al. (2008) BMC Genomics, 9:e463; Buchan et al. (2006) Nucleic Acids Res, 34: 1015-1027; Moura et al. (2007) PLoS ONE, 2(9):e847; each of which is incorporated herein by reference). Still other modifications can be made to the non-coding sequences of the ogt gene to enhance or control the expression of the gene encoding OGT polypeptide.

[00106] Conservative amino acid substitutions are amino acid substitution in which the substituted amino acid residue is of similar charge as the replaced residue and/or is of similar or smaller size than the replaced residue. Conservative substitutions of amino acids include substitutions made amongst amino acids within the following groups: (a) the small non-polar amino acids, A, M, I, L, and V; (b) the small polar amino acids, G, S, T, and C; (c) the amido amino acids, Q and N; (d) the aromatic amino acids, F, Y, and W; (e) the basic amino acids, K, R, and H; and (f) the acidic amino acids, E and D. Substitutions which are charge neutral and which replace a residue with a smaller residue may also be considered conservative substitutions even if the residues are in different groups (e.g., replacement of phenylalanine with the smaller isoleucine). Methods for making amino acid substitutions, additions, or deletions are well known in the art, e.g., polymerase chain reaction (PCR) -directed methods (Molecular Biology: Current Innovations and Future Trends, by Griffin A.M. and Griffin H.G. (1995) Horizon Scientific Press, Norfolk, U.K; Modern Genetic Analysis, by Griffith A. J., Second Edition, (2002) H. Freeman and Company, New York, NY).

[00107] Non-conservative substitutions, such as mutations of residues in the active site or other sites that reduce or inhibit OGT activity (e.g., mutations of wild-type amino acid residues to alanine, as provided in Table 3) may also be introduced. Using the detailed three-dimensional structural information provided herein the effect of non-conservative substitutions on the structure of OGT can be predicted. One skilled in the art will be able to predict the effect of a substitution by using the detailed three-dimensional structural information provided herein, as well as using routine biological screening assays. For a detailed description of protein chemistry and structure, see Principles of Protein Structure by Schulz, G. E. et al. (1979) Springer- Verlag, New York, and Proteins: Structure and Molecular Principles by Creighton, T. E. (1984) W. H. Freeman & Co., San Francisco.

[00108] OGT may be recombinantly produced using a vector (e.g., a pET24b vector) including a coding sequence operably associated with one or more regulatory sequences. A coding sequence and regulatory sequences are "operably associated with" when they are covalently linked to place the expression or transcription of the coding sequence under the control of the regulatory sequence. A promoter region is operably associated with to a coding sequence if the promoter region is capable of modulating transcription of the coding sequence.

[00109] The nature of the regulatory sequences needed for gene expression may vary between species or cell types but may generally include 5 '-non-transcribed and 5'- non-translated sequences involved with initiation of transcription and translation respectively, such as, for example, TATA box, capping sequence, and CAAT sequence. 5'-non-transcribed regulatory sequences may include a promoter region which includes a promoter sequence for transcriptional control of the operably associated gene. Promoters may be constitutive or inducible. Regulatory sequences may also include enhancer sequences or upstream activator sequences.

[00110] A DNA sequence operably associated with a regulatory sequence may be inserted by restriction and ligation into a vector, e.g., for transport between different genetic

environments or for expression in a host cell. Vectors are typically composed of DNA or RNA. Vectors include, but are not limited to, plasmids, viral vectors, cosmids, artificial chromosomes, and phagemids. A cloning vector is one which is able to replicate in a host cell, and which is further characterized by one or more endonuclease restriction sites at which the vector may be cut and into which a desired nucleic acid sequence (e.g., an open reading frame) may be inserted. Vectors may contain one or more marker sequences suitable for use in the identification of cells which have or have not been transformed or transfected with the vector. Markers include, for example, genes encoding proteins which increase or decrease either resistance or sensitivity to antibiotics or other compounds, genes which encode enzymes whose activities are detectable by standard assays known in the art (e.g. , β-galactosidase, alkaline phosphatase or luciferase), and genes which visibly affect the phenotype of transformed or transfected cells, hosts, colonies or plaques.

[00111] For prokaryotic systems, plasmid vectors that contain replication sites and control sequences derived from a species compatible with the host may be used. Preferably, the vector has the capacity to autonomously replicate in the host cell. Useful prokaryotic hosts include bacteria such as E. coli (e.g. BL21 (DE3)). To express OGT in a prokaryotic cell, it is desirable to operably join the nucleic acid sequence of OGT (e.g. cDNA) to a functional prokaryotic promoter. Such promoter may be either constitutive or regulatable (e.g. by induction or derepression). If expression of OGT in eukaryotic hosts is desired, such hosts may include, for example, yeast, fungi, insect cells, and mammalian cells. In addition, plant cells are also available as hosts, and control sequences compatible with plant cells are known in the art.

[00112] A wide variety of transcriptional and translational regulatory sequences may be employed depending upon the nature of the host. The transcriptional and translational regulatory signals may be derived from viral sources, such as adenovirus, bovine papilloma virus, and simian virus. Mammalian promoters, such as, for example, actin, collagen, and myosin promoters may be employed. Transcriptional initiation regulatory signals may be selected which allow for repression or activation, so that expression of the gene sequences can be modulated, for example, by regulatory signals, such as repression/initiation through changes in temperature or by addition of a chemical or biological modulating agent.

[00113] Vector can be employed which are capable of integrating a desired gene sequences into the host cell chromosome. Cells which have stably integrated the introduced nucleic acid into their chromosomes can be selected by also introducing one or more markers which allow for selection of host cells which contain the expression vector. The selectable marker gene sequence can either be directly linked to the gene sequences to be expressed, or introduced into the same cell by co-transfection. Additional elements, such as splice signals, transcription promoters, enhancers, and termination signals may also be needed for optimal synthesis of OGT mRNA.

[00114] Once a desired vector or desired nucleic acid sequence has been prepared, the vector or nucleic acid sequence is introduced into an appropriate host cell by any of a variety of suitable means, for example, transformation, transfection, conjugation, protoplast fusion, electroporation, calcium phosphate-precipitation, or direct microinjection. After the introduction of the vector, recipient cells are grown in a selective medium, which selects for the growth of vector-containing cells. Expression of the cloned gene sequence results in the production of recombinant OGT. The nucleic acid sequence of the final insert may optionally be verified by sequencing.

Over expression and purification of recombinant OGT

[00115] Wild- type OGT as well as mutated forms of OGT may be produced

recombinantly. Recombinant OGT can be expressed in various host systems. For example, the host system is E. coli, such as the E. coli strain is BL21 (DE3). Expression of recombinant OGT may be induced through activation of an inducible promoter {e.g., an IPTG-inducible promoter). Recombinant expression of OGT and isolation procedures of OGT, for example, from bacteria, may provide OGT polypeptide of sufficient quantity and quality to permit its identification, characterization, and/or use, for example, in protein crystallization, biochemical studies, in vitro compound screening, etc. The isolated polypeptide can be selectively produced by expression cloning and purified by techniques known in the art {e.g., chromatography, precipitation, electrophoresis). Such purification methods are well known in the art {Biochemistry by Zubay G., 2nd Edition (1988) Macmillan Publishing Co., New York, NY, USA; Protein Purification Handbook by Amersham Pharmacia Biotech, Edition AB (1999) Amersham Pharmacia Biotech Inc. New Jersey, USA; incorporated herein by reference). Recombinant OGT may be purified from bacteria as set forth in the Examples below. Recombinant OGT with a poly His tag, for example, may be purified using a Ni-NTA agarose superflow resin (QIAgen, Valencia, CA), followed by enzymatic cleavage of the N-terminal tags {e.g., using HRV 3C protease), (EMD, Gibbstown, NJ). Methods of purification may optionally employ chromatography to isolate the desired protein, e.g. gel filtration (e.g., Superdex200 column (GE Healthcare, Piscataway, NJ).

Biochemical characterization of recombinant OGT

[00116] Recombinant OGT may be characterized using techniques that are well known in the art. For example, recombinant human OGT (rhOGT) can be characterized by enzyme kinetic assays. For example, OGT activity may be measured using a filter-binding assay (Gross, B.J. et al. J Am Chem Soc 111, 14588-9 (2005)). Such assay may include CKII3K peptide

(KKKYPGGSTPVSSANMM, SEQ ID NO: 2), UDP-14C-GlcNAc, OGT (WT or mutant protein), and a reaction buffer. Reactions may be quenched by spotting onto a phosphocellulose discs. After washing, binding may be detected by liquid scintillation counting. Other biochemical assays may also be used, for example Zhang et al., A Modified Coupled Enzyme Method for O-linked GlcNAc Transferase Activity Assay, Biol Proced online 11(1): 170-183 (2009); and Leavya and Bertozzi, A high-throughput assay for O-GlcNAc transferase detects primary sequence preferences in peptide substrates, Bioorganic & Medicinal Chemistry Letters, 17(14): 3851-3854 (2007).

Crystallization Screening of OGT and Cryo-Optimization

[00117] The invention also provides methods for crystallizing OGT. In certain embodiments, methods for crystallizing OGT involve crystallizing purified recombinant OGT as described herein. In certain embodiments, purified recombinant OGT is ncOGT (amino acids 1- 1028), mOGT (amino acids 167-1028), or sOGT (amino acid 372-1028). In certain

embodiments, purified recombinant OGT is I1OGT4 5 (amino acids 313-1028). In certain embodiments, purified recombinant I1OGT4 5 (amino acids 313-1028) having the amino acid sequence set forth in SEQ ID NO: 54 or a fragment thereof is crystallized by the methods provided herein. In certain embodiments, methods for crystallizing OGT involve crystallizing fragments or portions of recombinant OGT as described herein (e.g., ncOGT, mOGT, hOGT, or sOGT) including or excluding one or more of the following domains: a) the C-Cat domain (amino acids 828-997); b) the N-Cat domain (amino acids 496-697); and/or c) the Int-D domain (amino acids 698-827). It should be appreciated that recombinant OGT may be crystallized by the methods provided herein that comprise any number of tetratricopeptide repeat (TPR) units, such as, e.g., one -half, one, two, three, four, five, six, seven, eight, nine, ten, eleven, twelve, or thirteen TPR units, and/or that comprises a portion or combination of any of the domains or units of (a) to (c).

[00118] In certain embodiments, the purified recombinant OGT that is crystallized comprises an amino acid sequence that has at least 60%, 65%, 70%, 75%, 80%, 85%, 90%, 95%, or 99% amino acid sequence homology or identity with the amino acid sequences set forth in SEQ ID NO: 53 and SEQ ID NO: 54, or a fragment thereof. In certain embodiments, the purified recombinant OGT that is crystallized is an OGT variant, such as, for example, an OGT mutant. Such mutant may comprise a mutation that reduces OGT activity. Examples of such mutants are described in Table 3. In certain embodiments, the purified recombinant OGT that is crystallized is a OGT variant that is an isoform, homolog, or ortholog of human OGT, such as a member of the OGT family, having significant amino acid sequence homology, such as having at least 60%, 65%, 70%, 75%, 80%, 85%, 90%, 95%, or 99% sequence homology, with the amino acid sequence set forth in SEQ ID NO: 53 or SEQ ID NO: 54,. In certain embodiments, methods for crystallizing OGT in form of a co-crystal are provided. For example, OGT or a fragment thereof may be co-crystallized with UDP-GlcNAc, UDP, or a variant thereof. OGT or a fragment thereof may also be co-crystallized with a peptide substrate or a variant thereof, for example, one of the peptide substrates set forth in Table 4. OGT or a fragment thereof may also be co-crystallized with a peptide substrate and UDP.

[00119] One of ordinary skill in the art will appreciate that a wide variety of crystallization conditions may be employed to provide crystals of OGT, therefore, a wide variety of

crystallization conditions are envisioned and encompassed by the present invention. Every protein crystallizes under a unique set of conditions, such as, for example, supersaturating the solution containing the protein; and/or adding precipitating or crystallizing agents, salts, metals, and/or buffers to the solution containing the protein.

[00120] Any crystallization technique known to those skilled in the art may be employed to obtain the crystals of the present invention, including, but not limited to, batch crystallization, vapor diffusion (e.g., either by sitting drop or hanging drop), and micro dialysis. Seeding in some instances may be required to obtain x-ray quality crystals. Standard micro and/or macro seeding of crystals may therefore be used. In certain embodiments, the crystals of the present invention are grown using the hanging-drop vapor-diffusion method. [00121] The crystals of OGT may be grown at any temperature suitable for crystallization.

For example, the crystals of OGT may be grown at temperatures ranging from approximately 0 °C to approximately 30 °C. In certain embodiments, the crystals of the present invention are grown at a temperature of between approximately 0 °C to approximately 10 °C. In certain embodiments, the crystals of the present invention are grown at a temperature of between approximately 0 °C to approximately 5 °C. In certain embodiments, the crystals of the present invention are grown at a temperature of between approximately 5 °C to approximately 10 °C. In certain embodiments, the crystals of the present invention are grown at a temperature of between approximately 10 °C to approximately 15 °C. In certain embodiments, the crystals of the present invention are grown at a temperature of between approximately 15 °C to

approximately 20 °C. In certain embodiments, the crystals of the present invention are grown at a temperature of between approximately 20 °C to approximately 25 °C. In certain

embodiments, the crystals of the present invention are grown at a temperature of between approximately 25 °C to approximately 30 °C. In certain embodiments, the crystals of the present invention are grown at a temperature of approximately 0 °C. In certain embodiments, the crystals of the present invention are grown at a temperature of approximately 1 °C. In certain embodiments, the crystals of the present invention are grown at a temperature of approximately 2 °C. In certain embodiments, the crystals of the present invention are grown at a temperature of approximately 3 °C. In certain embodiments, the crystals of the present invention are grown at a temperature of approximately 4 °C. In certain embodiments, the crystals of the present invention are grown at a temperature of approximately 5 °C. In certain embodiments, the crystals of the present invention are grown at a temperature of approximately 6 °C. In certain embodiments, the crystals of the present invention are grown at room temperature.

[00122] Crystals of OGT as provided by the present invention are typically grown from a crystallization solution comprising one or more precipitants. In certain embodiments the precipitants may be selected from polymers, polyethers, alcohols, salts, and/or polyols. In certain embodiments, these precipitants are selected from the group consisting of monomethyl ether (MME); polyethylene glycol PEG-400; PEG- 1000; PEG-2000; PEG-3000; PEG-8000; PEG 20,000; ((NH4)2S04); 2-propanol; 1,4-butanediol; K/Na tartrate; ethanol; NaCl; sodium citrate; NaH2P04/K2HP04; ethylene glycol; dioxane; 2-methyl-2,4-pentanediol (MPD);

polyethyleneimine; tert-butanol; and 1,6-hexanediol. [00123] In certain embodiments, the crystallization conditions may further comprise one or more salts. Thus, in certain embodiments the crystallization conditions further comprises one or more salts selected from the group consisting of MgCl2, Zn(OAc)2, Li2S04, Ca(OAc)2, NaCl; (NH4)2 S04, CdCl2, CoCl2, MgS04, and NiCl2. In certain embodiments, the crystallization conditions further comprises one or more buffers selected from the group consisting of 2- (cyclohexylamino)ethanesulfonic acid (CHES); 2-(N-morpholino)ethanesulfonic acid (MES); N- cyclohexyl-3-aminopropanesulfonic acid (CAPS); N-cyclohexyl-2-hydroxyl3- aminopropanesulfonic acid (CASPO); 4-(2-hydroxyethyl)piperazine-l-ethanesulfonic acid (HEPES); 3-(N-morpholino)propanesulfonic acid (MOPS); 2-amino-2-(hydroxymethyl)-l,3- propanediol (Tris); piperazine-N,N'-bis(2-ethanesulfonic acid) (PIPES); N-(2-Acetamido)-2- aminoethanesulfonic acid (ACES); N,N-Bis(2-hydroxyethyl)-2-aminoethanesulfonic acid (BES); N-Tris(hydroxymethyl)methyl-2-aminoethanesulfonic acid (TES); N-(2-acetamido)iminodiacetic acid (ADA); tris(2-carboxylethyl)phosphine (TCEP); acetamido glycine; cholamine chloride; glycinamide; bicine; N-(2-Hydroxy-l,l-bis(hydroxymethyl)ethyl)glycine (tricine); imidazole; sodium citrate; sodium acetate; cacodylate; Na/K phosphate, and buffers as described in Good et ah, Biochemistry 5:467-477 (1966), which is incorporated herein by reference.

[00124] In certain embodiments, the pH of the crystallization solution is between a pH of approximately 3 to a pH of approximately 9. In certain embodiments, the pH of the

crystallization solution is a pH of approximately 7.0.

[00125] In a specific embodiment, crystals are grown with the hanging drop method at room temperature. In a specific embodiment, to obtain crystals comprising hOGT4 5 and UDP and the reservoir solution contains 1.45 M potassium phosphate (dibasic), 8 mM EDTA, and 1% xylitol. In a specific embodiment, to obtain crystals comprising hOGT4 5, UDP, and CKII3K peptide (Kreppel et ah, J Biol Chem 274, 32015-22 (1999), Gross et ah, J Am Chem Soc 127, 14588-9 (2005)), the reservoir reservoir solution contains 1.6 M Li2S04 and 0.1M Bis Tris Propane, pH 7.0.

[00126] In certain embodiments, the crystals are flash frozen using a cryoprotectant. In certain embodiments, cryoprotectant may comprise a) salts and/or buffers that are similar or identical (in kind and/or concentration) to the salts and/or buffers in which crystallization of the protein occurs, and b) 20-35% v/v of polyols, such as glycerol, ethylene glycol, or 2-methyl-2,4- pentanediol (MPD), or 15-70% w/v of sugars, such as sucrose or xylitol. Crystals may be soaked in the cryo-buffer for about 5-15 minutes. In a specific embodiment, cryo-protection of binary OGT co-crystal (comprising I1OGT4.5 and UDP) grown in 1.45 M potassium phosphate dibasic, 8 mM EDTA, and 1% xylitol is achieved by soaking the crystals in a cryo-buffer containing 1.8 M potassium phosphate and 27% xylitol. Crystals protected with this cryo-buffer diffracted to 2.8

A. In other embodiment cryo-protection of ternary OGT crystals (comprising hOGT4 5,UDP, and CKII3K peptide) grown in 1.6 M Li2S04 and 0.1M Bis Tris Propane (pH 7) is achieved by soaking the crystals in a cryo-buffer containing 1.72 M Li2S04, 0.05 M Bis Tris Propane, (pH

7.0), and 28% xylitol. Crystals protected with this cryo-buffer diffracted to 1.95 A.

[00127] OGT crystals may also include a binding compound bound to the OGT polypeptide. The complex of the polypeptide and binding compound may be formed before, after, or during crystallization. In a specific embodiment with crystals comprising hOGT4 5 and UDP, OGT is incubated with UDP for several hours at 4 °C prior to crystallization. In another embodiment with crystals comprising hOGT4 5, UDP, and CKII3K peptide, OGT is incubated with UDP and CKII3K peptide for several hours at 4 °C prior to crystallization. In certain embodiments, the crystals of the present invention and the crystallization conditions further comprise a binding compound. Thus, in certain embodiments, the crystallization solution of the above method further comprises a binding compound in order to provide an OGT-binding compound complex, such as, for example, the binary or ternary complex provided herein.

[00128] In certain embodiments, an OGT crystal provided by the above method is soaked in a solution of a binding compound (other than UDP-based compounds and/or peptide substrates) to provide a OGT-binding compound complex. In certain embodiments, the binding compound is bound in the active site of OGT. In certain embodiments, the binding compound is a small molecule. The small molecule may, for example, be a quinolinone or

dihydroquinolinone as described in U.S. Patent Application, U.S. S.N. 61/217,514, filed June 1, 2009, which is incorporated herein by reference. In certain embodiments, the binding compound is of the formula (I):

wherein:

= denotes a single or double bond;

R1 is cyclic or acyclic, substituted or unsubstituted, branched or unbranched aliphatic; cyclic or acyclic, substituted or unsubstituted, branched or unbranched heteroaliphatic; substituted or unsubstituted aryl; substituted or unsubstituted heteroaryl; substituted or unsubstituted, branched or unbranched arylalkyl; or substituted or unsubstituted, branched or unbranched heteroarylalkyl;

2 and R 3J are independently hydrogen; cyclic or acyclic, substituted or unsubstituted, branched or unbranched aliphatic; cyclic or acyclic, substituted or unsubstituted, branched or unbranched heteroaliphatic; substituted or unsubstituted, branched or unbranched acyl;

substituted or unsubstituted aryl; substituted or unsubstituted heteroaryl; substituted or unsubstituted, branched or unbranched arylalkyl; substituted or unsubstituted, branched or

B B B B

unbranched heteroarylalkyl; -C(=0)R ; -SOR ; -S02R ; or -C(R )3; wherein each occurrence of R is independently hydrogen; halogen; a protecting group; aliphatic; heteroaliphatic; acyl; aryl; heteroaryl; alkoxy; aryloxy; amino; alkylamino; dialkylamino; or heteroaryloxy; or

R 2" and R 3J may optionally be taken together with the intervening nitrogen to form a saturated or unsaturated, substituted or unsubstituted heterocyclic moiety;

R4 is hydrogen, C1-6 aliphatic, or a protecting group;

R5 is hydrogen, C1-6 aliphatic, or a protecting group;

R6 is hydrogen; halogen; cyclic or acyclic, substituted or unsubstituted, branched or unbranched aliphatic; cyclic or acyclic, substituted or unsubstituted, branched or unbranched heteroaliphatic; substituted or unsubstituted, branched or unbranched acyl; substituted or unsubstituted, branched or unbranched aryl; substituted or unsubstituted, branched or unbranched heteroaryl; -ORF; -C(=0)RF; -C02RF; -C(=0)N(RF)2; -CN; -SCN; -SRF; -SORF; -S02RF; -N02; -

F F F F

N(R")2; -NHC(0)R"; or -C(Rr)3; wherein each occurrence of R is independently hydrogen; halogen; a protecting group; aliphatic; heteroaliphatic; acyl; aryl moiety; heteroaryl; alkoxy; aryloxy; alkylthioxy; arylthioxy; amino; alkylamino; dialkylamino; heteroaryloxy; or

heteroarylthioxy; and

n is 0, 1, 2, or 3; and a pharmaceutically acceptable salt.

[00129] In certain embodiments, the small molecule does not include a quinolinone or dihydroquinolinone core. In some embodiments, the small molecule is a modulator of OGT activity, for example, an inhibitor of OGT activity. In some embodiments, the inhibitor is a reversible inhibitor. In certain embodiments, the inhibitor is a non-reversible inhibitor.

Crystallizable Compositions of OGT

[00130] The present invention also provides crystallizable compositions of OGT and variants thereof. The term "crystallizable composition" as used herein refers to a composition comprising OGT or a variant thereof that may be used to produce a crystal of OGT or a variant thereof using methods described herein or known in the art. In certain embodiments, a crystallizable composition comprises a mammalian OGT, such as mouse or rat OGT. In certain embodiments, a crystallizable composition comprises human OGT. In certain embodiments, a crystallizable composition comprises an ortholog of human OGT. In certain embodiments, a crystallizable composition comprises non-mammalian OGT, such as bacterial OGT or plant OGT. In certain embodiments, the a crystallizable composition comprises an OGT isoform, such as sOGT, mOGT, or ncOGT. In certain embodiments a crystallizable composition comprises a mutant OGT. In certain embodiments, a crystallizable composition comprises hOGT4 5, or any structural modification thereof. In certain embodiments, a crystallizable composition comprises native OGT. In certain embodiments, a crystallizable composition comprises hOGT4 5 and UDP. In certain embodiments, a crystallizable composition comprises hOGT4 5, UDP, and CKII3K peptide. A crystallizable composition of the present invention may produce a variety of crystalline forms, all of which are contemplated by the present invention.

Crystals of OGT

[00131] The present invention also provides crystals of OGT and variants thereof. In certain embodiments, the crystals are of a mammalian OGT, such as mouse or rat OGT. In certain embodiments, the crystals are of human OGT. In certain embodiments, the crystals are of an ortholog of human OGT. In certain embodiments, the crystals are of non-mammalian OGT, such as bacterial OGT or plant OGT. In certain embodiments, the crystals are of an OGT isoform, such as sOGT, mOGT, or ncOGT. In certain embodiments, the crystals are of a mutant OGT. In certain embodiments, the crystals are of hOGT4 5, or any structural modifications thereof. In certain embodiments, the crystals are of native OGT. In certain embodiments, the crystals are of a binary complex of OGT complex comprising hOGT4 5 and UDP. In certain embodiments, the crystals are of a ternary OGT complex comprising I1OGT4.5, UDP, and CKII3K peptide. A crystal of the present invention may take a variety of forms, all of which are contemplated by the present invention. In certain embodiments, the crystal may have a size of about 100x20x20 microns, about 150x50x50 microns, about 200x50x50 microns, about

300x50x50 microns or 400x100x100 microns. In certain embodiments, the crystals grow as hexagonal rods (e.g. I1OGT4 5 and UDP ) or as trapezoidal crystals (e.g. I1OGT4 5, UDP, and CKII3K peptide). In certain embodiments, the trapezoidal crystals have the space group 1121 and the unit cell parameters a=98.538 A, b=136.66 A, c=153.54 A and bond angles α= γ=90°, β= 102.90°. In certain embodiments, the hexagonal rod crystals have the space group P321 and the unit cell parameters a=b=273.6592 A, c=143.0501 A and bond angles α=β= 90°, γ=120°. In certain embodiments, the crystal diffracts x-rays for a determination of structural coordinates to a maximum resolution of about 2.8 A, for example for a binary OGT complex of I1OGT4 5 and

UDP. The crystals may diffract to a maximum resolution of about 1.95 A, for example for a ternary OGT complex of hOGT4.5,UDP, and a peptide substrate.

Crystal structure of OGT

[00132] Three-dimensional structural information for human OGT including binding compounds (e.g. UDP, UDP-GlcNAc, and a peptide substrate), are provided. This structural information may be used to predict the structure of OGT variants, for example, those set forth in Table 3, variants that are isoforms, homologs, or orthologs of hOGT, variants that comprise one or more posttranslational modifications, or variants that are fragments of full-length OGT (amino acids 1-1028), e.g. amino acids: 1-997, 1-828, 1-827, 1-698, 1-697, 1-496, 167-1028, 167-997, 167-828, 167-827, 167-698, 167-697, 167-496, 313-1028, 313-997, 313-828, 313-827, 313-698, 313-697, 313-496, 372-1028, 372-997, 372-828, 372-827, 372-698, 372-697, 372-496, 466- 1028, 466-997, 466-828, 466-827, 466-698, 466-697, 466-496, 496-1028, 496-997, 496-828, 496-827, 496-698, 496-697, 697-1028, 697-997, 697-828, 697-827, 698-1028, 698-997, 698- 828, 698-827, 827-1028, 827-997, 828-1028, 828-997, and 997-1028. In certain embodiments, the invention provides methods for constructing models of these variants using the three- dimensional structural information of human OGT as a template. The method may include adjusting the backbone dihedral angles and the side chains of each amino acid that is modeled until a low energy conformation is obtained. [00133] In certain embodiments, x-ray diffraction data collection can be performed in an x-ray crystallography facility. One, two, three, or more diffraction data sets may be collected from one or more OGT crystals. In certain embodiments, the crystals of the present invention diffract to a resolution limit of at least approximately 4 angstrom (A). In certain embodiments, the crystals diffract to a resolution limit of at least approximately 3 A. In certain embodiments, the crystals diffract to a resolution limit of at least approximately 2 A. In certain embodiments, the crystals diffract to a resolution limit of at least approximately 1.5 A. In certain embodiments, the crystal diffracts x-rays for a determination of structural coordinates to a maximum resolution of about 2.8 A, for example for a binary OGT complex of I1OGT4 5 and UDP. The crystals may diffract to a maximum resolution of about 1.95 A, for example for a ternary OGT complex of I1OGT4 5,UDP, and a peptide substrate.

Diffraction data can be collected using variable oscillation angles, number of frames, and exposure times that all depend on the equipment used and on the quality of the crystals used to collect the data. One of ordinary skill would know how to optimize these parameters {Principles of protein X-ray crystallography by J. Drenth. 2nd ed. (1999) Springer- Verlag, Heidelberg, Germany; Structure Determination by X-ray Crystallography by M. Ladd and R. Palmer. 4th ed. (2003) Kluwer Academic/Plenum Publishers, New York, NY). For example, diffraction data can be collected with 0.1°, 0.3°, 0.5°, 1°, 1.5°, 2°, 3°, 4°, 5°, or 10° oscillation, or any oscillation angle in between these angles, collecting, for example, 10, 20, 50, 100, 200, 300. 400, 500, 1000, or 5000 frames, or any number of frames in between these numbers. Various frame exposure times may be used, such as, for example 5 seconds, 10 seconds, 20 seconds, 30 seconds, 40 seconds, 50 seconds, 60 seconds, 120 seconds, 180 seconds, 3 minutes, 4 minutes, 10 minutes, 20 minutes, 30 minutes per frame or any exposure time in between these times. Data merging and scaling can be done, for example, using commercially available software suites. Structure determination, model building, and refinement can be performed, for example using iMosflm (Leslie, Recent changes to the MOSFLM package for processing film and image plate data. Joint CCP4 + ESF-EAMCB Newsletter on Protein Crystallography 26(1992)), SCALA (Evans, Scaling and assessment of data quality. Acta Crystallogr D Biol Crystallogr 62, 72-82 (2006)), HKL2MAP (Pape et al., J Appl. Cryst. 37, 843-844 (2004)), Phaser (McCoy et al., JAppl Crystallogr 40, 658-674 (2007)), (molecular replacement module (McCoy, Acta Crystallogr D Biol Crystallogr 63, 32-41 (2007))) and FFT CCP4 (The CCP4 suite: programs for protein crystallography, Acta Crystallogr D Biol Crystallogr 50, 760-3 (1994)) programs, MIRAS phasing with the program SHARP (de la Fortelle et al, Methods Enzymol 276, 472-494 (1997)) for the native data sets and the heavy atom derivative data sets. The structure may be refined with, for example, Molrep, Refmac, CNS (Brunger et al., Acta Crystallogr D Biol Crystallogr 54, 905-21 (1998)), COOT (Emsley et al., Acta Crystallogr D Biol Crystallogr 60, 2126-32 (2004)), Phenix (Adams et al., Acta Crystallogr D Biol Crystallogr 66, 213-21) and TLS refinement (Painter et al., J. Appl. Cryst. 39, 109-111 (2006), Painter et al., Acta Crystallogr D Biol Crystallogr 62, 439-50 (2006)). For visualization Pymol (DeLano, The Pymol Molecular Graphics System, (Delano Scientific, San Carlos, CA, USA, 2002)) (pymol.org; molecular viewer software) and CCP4mg (Potterton et al., Acta Crystallogr D Biol Crystallogr 60, 2288-94 (2004)) (CCP4 program suite (www.ccp4.ac.uk)). may be used.

[00134] The term "molecular replacement" refers to a method that involves generating a preliminary model of the three-dimensional structure of OGT or a OGT complexed with a binding compound whose structure coordinates are not known by orienting and positioning an OGT structure whose atomic coordinates are known (for example, based on the atomic coordinates provided in Tables 5, 6, and 7). Phases are calculated from this model and combined with the observed amplitudes of the unknown crystal structure to give an approximate structure. This structure is then subject to any of several forms of refinement to provide a final, accurate structure. Any program known to the skilled artisan may be employed to determine the structure by molecular replacement. Suitable molecular replacement programs include, but are not limited to, AMORE (1994) (the CCP4 suite: Acta Crystallogr. D., 50:760-763; Navaza (1994) Acta Cryst., A50: 157-163) and CNS (1998) (Acta Crystallogr. D., 54:905- 921).

[00135] In certain embodiments, the atomic coordinates of crystalline OGT are provided.

In one embodiment, wherein the crystal diffracts to a resolution of approximately 2.8 A the model may be refined to a final R factor of 17.4% and Rfree of 22.3% (for example for the binary OGT complex comprising hOGT4 5 and UDP). In one embodiment, wherein the crystal diffracts to a resolution of -2.4 A the model may be refined to a final R factor of 22.4% and Rfree of 25.2% (for example, for the ternary OGT complex of hOGT4 5,UDP, and (CKII3K peptide). In certain embodiments, atomic coordinates of a crystalline OGT binary and ternary complex are provided, and the parameters are set forth in Table 5 and Table 6, respectively. In one embodiment, the crystalline binary complex of OGT at 2.8 A has a space group of P321 and has unit cell parameters of a = b =273.6592 A, c=143.0501 A and bond angles of α=β=90°, γ=120°.

In another embodiment, the crystalline ternary complex of OGT at 1.95 A has a space group of 1121 and has the unit cell parameters of a = 98.538 A, b = 136.66 A, c = 153.54 A, α = γ = 90° and β =102.90°. The parameters for the OGT binary and ternary complex are set forth in Tables 1 and 2.

[00136] Crystalline OGT has four domains: a) the C-Cat domain (amino acids 828-997), b) the N-Cat domain (amino acids 496-697), c) the Int-D domain (amino acids 698-827), and d) a tetratricopeptide repeat (TPR) unit containing up to 13 TRP units (as depicted in Figure la). The catalytic region contains three domains: the N-terminal domain (N-Cat), the C-terminal domain (C-Cat), and an intervening domain (Int-D). The N-Cat domain contains two helices that form an essential part of the active site. The intervening sequence folds into a domain (depicted in Figure 9) that packs exclusively against the C-Cat domain. The C-Cat, N-Cat, UDP moiety, peptide substrate interface (pocket, cleft, entrance) and the catalytic core are depicted in Figures la-c, 2a-c, 2e, 6, and 7. The core of the OGT active site includes residues H498 and K842. The active site of OGT, the peptide substrate binding site (e.g. , H558 and N458) and the binding site of the UDP moiety further comprise D431, N458, H499, D523, H558, T560, R637, L653, Q839, K842, K898, H901, H920, T921, and D925. The three-dimensional structure of the active site of human OGT is provided by the atomic coordinates listed in Table 5 (binary complex of OGT and UDP), Table 6 (ternary complex of OGT, UDP, and peptide substrate), and Table 7 (ternary complex of OGT, UDP, and glycopeptide).

[00137] While Tables 5, 6, and 7 provide atomic coordinates for crystalline OGT, the present invention also contemplates structural modifications thereof, for example, mutants that have reduced OGT activity (for example, those set forth in Table 3) and isoforms, homologs or orthologs, and naturally occurring mutants of human OGT having significant structural homology (e.g., significant structural overlap), particularly in the areas recognized as active, and thus providing the same or similar structural information as provided herewith. Significant structural homology refers to at least one of the following criteria: (i) at least 60%, 65%, 70%, 75%, 80%, 85%, 90%, 95%, or 99% structural homology with crystalline OGT; or (ii) at least 60%, 65%, 70%, 75%, 80%, 85%, 90%, 95%, or 99% structural homology with a recognized active binding site of crystalline OGT. In certain embodiments, significant structural homology may also refer to at least 60%, 65%, 70%, 75%, 80%, 85%, 90%, 95%, or 99% structural homology with the primary amino acid sequence of an OGT (e.g.. human OGT). Furthermore, the primary amino acid sequence of OGT may be a sequence included as a segment in a larger amino acid sequence or may be a fragment thereof. Fragments include fragments that contain all or part of the following domains: a) the C-Cat domain (amino acids 828-997), b) the N-Cat domain (amino acids 496-697), c) the Int-D domain (amino acids 698-827), and d) a

tetratricopeptide repeat (TPR) unit containing up to 13 TRP units (as depicted in Figure la) and all of the following fragments: amino acids 1-997, 1-828, 1-827, 1-698, 1-697, 1-496, 167-1028, 167-997, 167-828, 167-827, 167-698, 167-697, 167-496, 313-1028, 313-997, 313-828, 313-827, 313-698, 313-697, 313-496, 372-1028, 372-997, 372-828, 372-827, 372-698, 372-697, 372-496, 466-1028, 466-997, 466-828, 466-827, 466-698, 466-697, 466-496, 496-1028, 496-997, 496- 828, 496-827, 496-698, 496-697, 697-1028, 697-997, 697-828, 697-827, 698-1028, 698-997, 698-828, 698-827, 827-1028, 827-997, 828-1028, 828-997, and 997-1028 of full-length ncOGT (amino acids 1-1028, as depicted in Figure la). The present invention contemplates any and all such variations and modifications of OGT.

Uses of OGT structural information

[00138] In another aspect, the invention provides methods and/or uses of OGT structural information, for example, methods for designing, identifying, and/or screening compounds that bind to OGT. Such compounds may be useful in treating diseases, associated with hyper-O- GlcNAcylation, such as diabetes and complications thereof, cancers, neurodegenerative diseases, autoimmune diseases, and inflammatory diseases. Any binding compounds (such as inhibitors, activators, etc.) may be designed in silico based on the three-dimensional structural information provided by the atomic coordinates described herein (for example, provided in Tables 5, 6, and 7). The compound may affect aspects of enzymatic function, such as substrate recognition and/or OGT catalytic activity. In certain embodiments, methods are provided for the in silico design, identification, and/or screening of OGT-binding compounds using the three-dimensional structural information provided herein. In certain embodiments, methods are provided that can be used to identify inhibitors, reversible inhibitors and activators of OGT activity. In certain embodiments, methods are provided that can be used to test potential binding compounds for their ability to bind to or to modulate OGT activity. These methods include in silico, in vitro, and in vivo methods. In certain embodiments, methods are provided for solving the structure of OGT isoforms, homologs, or orthologs using the three dimensional structural information provided herein. In certain embodiments, methods are provided, solving the (partial) structure of proteins comprising structurally or functionally homologous domains using the three- dimensional structural information for OGT provided herein.

[00139] The three-dimensional structural information provided herein will aid in the identification, characterization, and/or design of specific OGT-binding compounds. These compounds may have the ability to inhibit OGT activity. Novel compounds identified by the methods provided herein may be used to inhibit O-GlcNAc transferase (OGT) activity in a cell. O-GlcNAcylation by OGT refers to the glycosylation of serine and/or threonine residues on nuclear and cytoplasmic proteins that is catalyzed by OGT.

[00140] The atomic coordinates of OGT (Tables 5, 6, and 7) may be used to design, identify, and screen potential compounds for ones that bind to OGT, or isoforms, homolog, orthologs, and mutants thereof, and that alter OGT's physical, chemical, and/or physiological properties. Compounds obtained from such screening may further be tested for their ability to inhibit O-GlcNAcylation. Such testing may be done in vitro, for example, in assays involving in cell lines expressing OGT or in biochemical assays. In another embodiment, compounds obtained from such screens may be tested for their ability to treat diabetes and complications thereof prolif. diseases, cancers, neurodegenerative diseases, autoimmune diseases, and inflammatory diseases in a subject, such as a mammal, e.g., a human, a pet (dog, cat, hamster, etc.), a farm animal (cow, sheep, camel, pig, etc.).

[00141] The atomic coordinates of OGT (Tables 5, 6, and 7) can be used to

computationally screen for small molecules that bind to OGT and/or a OGT family member in order to select, design, and/or develop compounds that bind to OGT and/or an OGT family member. A binding compound according to this invention may bind to an active site or any other site which is not identified on OGT. In certain embodiments, the binding compound is an inhibitor or activator of OGT activity. In certain embodiments, the inhibitor is a competitive, uncompetitive or non-competitive inhibitor. In certain embodiments, the inhibitor is a reversible inhibitor. Those of skill in the art may identify inhibitors as competitive, uncompetitive or noncompetitive or reversible inhibitors by computer fitting enzyme kinetic data using standard equations according to, for example, Enzyme Kinetics by Segel (1975) J. Wiley & Sons, incorporated herein by reference, or by employing assays which measure the ability of a potential inhibitor to OGT enzymatic activity (e.g., O-GlcNAcylation by OGT of serine and/or threonine residues). Inhibitors may comprise a quinolinone or dihydroquinolinone core, as described in U.S. Patent Application U.S. S.N: 61/217,514, filed June 1, 2009, or may be novel compounds of a different chemical structure or class.

[00142] In one embodiment, the present invention provides a method for the design and identification of a binding compound for OGT and/or an OGT family member, isoform, homolog, ortholog, or mutant, comprising the steps of: (a) using a three-dimensional structure of OGT as defined by the atomic coordinates provided in Tables 5, 6, and/or 7; (b) employing the three-dimensional structure to design and/or select a binding compound; and (c) synthesizing and/or choosing the binding compound for testing, e.g. biochemical testing in vitro, biological testing in cell culture, laboratory animals, and/or humans.

[00143] Suitable computer programs which may be used in the design and selection of potential binding compounds (e.g., by selecting suitable chemical fragments) include, but are not limited to, GRID (Goodford (1985) /. Med. Chem. 28:849 857); MCSS (Miranker, A. and M. Karplus, (1991) Proteins: Structure. Function and Genetics, 11:29-34); AUTODOCK (Goodsell, D. S, and A. J. Olsen (1990) Proteins: Structure. Function, and Genetics 8: 195 202); and DOCK (Kuntz et al. (1982) /. Mol. Biol. 161:269-288), each of which is incorporated herein by reference.

[00144] Suitable computer programs which may be used in connecting the individual chemical entities or fragments include, but are not limited to, CAVEAT (Bartlett, (1989) Molecular Recognition in Chemical and Biological Problems, Special Pub., Royal Chem. Soc. 78: 182-196); and 3D Database systems such as MACCS-3D by MDL Information Systems, San Leandro, Calif.), HOOK (Molecular Simulations, Burlington, Mass.) and as reviewed in Martin, Y. C, (1992) /. Med. Chem. 35:2145 2154), each of which is hereby incorporated herein by reference.

[00145] In addition to the method of building or identifying a potential binding compound in a step-wise fashion (e.g., one fragment or chemical entity at a time as described above), potential binding compounds may be designed as a whole or "de novo" using either an empty active site or, optionally, including some portion of a known inhibitor, activator or binding compound. Suitable computer programs include, but are not limited to, LUDI (Bohm, (1992) /. Comp. Aid. Molec. Design 6:61-78); LEGEND (Nishibata, Y. and A. Itai, (1991) Tetrahedron 47:8985); and LEAPFROG (Tripos Associates, St. Louis, Mo.). Other molecular modeling techniques may also be employed in accordance with this invention; see, for example, Cohen, N. C. et al. (1990) J. Med. Chem. 33: 883-894, and Navia (1992) Current Opinions in Structural Biology 2:202-210; each of which is hereby incorporated herein by reference.

[00146] Once a binding compound has been designed, selected, identified, synthesized, or chosen by the methods described herein, the affinity with which that compound binds to OGT, a OGT family member, isoform, homolog, ortholog, or mutant, may be tested by computational or biochemical evaluation. A compound designed, or selected, or synthesized, or chosen as a binding compound may be further computationally optimized so that in its bound state it would preferably lack repulsive interactions with the target site. Such non-complementary {e.g., electrostatic) interactions include repulsive charge-charge, dipole-dipole, and charge-dipole interactions. Specifically, the sum of all electrostatic interactions between the potential binding compound and the site at which it is bound to OGT, a OGT family member, isoform, homolog, ortholog, or mutant, in certain embodiments, make a neutral or favorable contribution to the enthalpy of binding. Suitable computer software which may be used to evaluate compound deformation energy and electrostatic interactions, includes, but is not limited to, Gaussian 92, revision C by M. J. Frisch, Gaussian, Inc., (1992) Pittsburgh, Pa.; AMBER, version 4.0 by P. A. Kollman, (1994) University of California at San Francisco; QUANTA/CHARMM by Molecular Simulations, Inc., (1994) Burlington, Mass.; and Insight II/Discover by Biosysm Technologies Inc., (1994) San Diego, Calif. Other software packages will be known to those skilled in the art.

[00147] In certain embodiments, binding compounds may be specifically designed, selected, synthesized, and/or chosen by the above methods to induce non-complementary {e.g., electrostatic) interactions, such as repulsive charge-charge, dipole-dipole, and charge-dipole interactions. In certain embodiments, the sum of all electrostatic interactions between the potential binding compound and the site at which it is bound to OGT or a OGT family member make a contribution to the enthalpy of binding that is not neutral.

[00148] In certain embodiments, the above method comprises using a suitable computer program in designing and/or selecting a binding compound.

[00149] Additionally, in certain embodiments, the above method comprises using a suitable computer program in conjunction with synthesizing and/or choosing the binding compound. [00150] Furthermore, in certain embodiments, the above method further identified the steps of using a suitable assay, as described herein, to characterize the binding compound's influence on OGT activity. In certain embodiments, the above method further comprises: (d) contacting the potential binding compound with OGT in the presence of a substrate; and (e) determining the amount of substrate conversion by OGT, to OGT without the compound to determine the effect of the binding compound on OGT enzymatic activity. In certain

embodiments, the above method further comprises the steps of: (d) contacting the binding compound with a cell that exhibits OGT activity; and (e) determining the effect of the binding compound on OGT activity in the cell.

[00151] The invention also provides methods for solving the structures of other proteins which are OGT family members, OGT isoforms, homologs, orthologs or mutants, e.g. that comprise one or more mutations (as referenced in Table 3), such as missense, nonsense, and/or deletion mutations that may be associated with the reduction or loss of OGT activity. Structures of crystallized proteins comprising such alterations in the primary amino acid sequence as well as OGT orthologs or homologs of other organisms sharing some sequence homology and/or identity to the primary amino acid sequence of human OGT may be solved by molecular replacement with OGT structural information provided by the present invention (Tables 5, 6, and 7).

[00152] In certain embodiments, the present invention provides a method for solving the structure of OGT, mutated OGT, a OGT family member, an OGT isoform, homolog, or ortholog comprising the steps of: (a) collecting x-ray diffraction data of an OGT crystal complexed to a binding compound, an OGT mutant crystal, a OGT-family member crystal, or a crystal of an OGT isoform, homolog, or ortholog; (b) using the atomic coordinates of OGT according to Tables 5, 6, or 7 to perform molecular replacement with the x-ray diffraction data of the OGT crystal complexed to a binding compound, an OGT mutant crystal, an OGT-family member crystal or a crystal of an OGT isoform, homolog, or ortholog; and (c) determining the structure of the OGT crystal complexed to a binding compound, an OGT mutant crystal, a OGT-family member crystal or a crystal of a OGT isoform, homolog, or ortholog.

[00153] Additionally, the present invention provides methods of evaluating the binding properties of a binding compound comprising the steps of: (a) soaking a potential binding compound with crystalline OGT, to provide a crystalline OGT complexed to a binding compound; (b) determining the three-dimensional structure of the crystalline OGT complexed to the binding compound, by molecular replacement using the three-dimensional structure of OGT as defined by atomic coordinates according to Tables 5, 6, or 7; and (c) analyzing the three- dimensional structure of the crystalline OGT complexed to the binding compound, to the unbound binding compound to evaluate the binding characteristics of the binding compound. To evaluate binding properties of such compounds, assays may be used, such as, calorimetric techniques (e.g., isothermal titration calometry, differential scanning calometry), or Biacore™ can be used for initial screening. Other assays are known in the art. For further optimization, co-crystallization may be useful to determine the structure of OGT-binding compound complexes. For example, as binary or ternary complexes of OGT.

[00154] The invention also provides methods for solving the structures of other proteins which comprise protein domains of similar function, other homology domains, or proteins that comprise amino acid sequences of high homology or identity. Such protein structures may be solved using some or all of the structural information provided in Tables 5, 6, and 7. In some embodiments, molecular replacement methods may be employed to solve such structures using the structural information provided by the present invention (Tables 5, 6, and 7).

[00155] In another aspect, the present invention provides methods of treatment comprising administering a compound, identified by the screening methods using the three- dimensional structural information of OGT provided herein, to a subject. The identified compounds or pharmaceutical compositions thereof may be used to treat any disease including diabetes and complications thereof, insulin resistance, neurodegenerative diseases such as Alzheimer's disease, prolif. disease, cancer, autoimmune diseases, and inflammatory diseases. The compounds may be used to treat disease in humans and other animals including

domesticated or experimental animals. The compounds may also be used as probes of biological pathways.

[00156] In yet another aspect, the present invention provides pharmaceutical

compositions comprising the compounds identified by the screening methods using the three- dimensional structural information of OGT provided herein. Compounds and compositions thereof may be useful for the inhibition of the activity of O-GlcNAc transferase (OGT). OGT has been implicated in diabetes and complications thereof, cancers, neurodegenerative diseases, autoimmune diseases, and inflammatory diseases (Golks et ah, EMBO Reports (2008) 9: 748- 753; Liu et al, Proc. Natl. Acad. Sci. USA (2004) 101: 10804-10809; Jones, Circulation

Research (2005) 96: 925-926; Golks et al., EMBO J. (2007) 26: 4369-4379; Ohn et al., Nature Cell Biol. (2008) 10: 1224-1231). The composition typically comprises a therapeutically effective amount of the identified compound to inhibit OGT and/or treat diabetes and

complications thereof, insulin resistance, neurodegenerative diseases such as Alzheimer' s disease, prolif. disease, cancer, autoimmune diseases, and inflammatory diseases. The pharmaceutical compositions may optionally include a pharmaceutically acceptable excipient. Any mode of administration including oral, parenteral, and topical administration of the inventive compound or pharmaceutical compositions thereof may be used.

[00157] The identified compounds and formulated pharmaceutical compositions may be used in treating or preventing any disease or condition including, but not limited to, diabetes and complications thereof, proliferative diseases (e.g., cancer, benign neoplasms, diabetic retinopathy), neurodegenerative diseases, autoimmune diseases (e.g., rheumatoid arthritis, lupus, multiple sclerosis), and inflammatory diseases. The compounds and pharmaceutical

compositions thereof may be administered to animals, preferably mammals (e.g., domesticated animals, cats, dogs, mice, rats), and more preferably humans. Any method of administration may be used to deliver the inventive compound or pharmaceutical composition thereof to the animal. In certain embodiments, the compound or pharmaceutical composition is administered orally. In other embodiments, the compound or pharmaceutical composition is administered parenterally.

[00158] In certain embodiments, the compounds may be used for treating or lessening the severity of diabetes and complications thereof including, but not limited to, diabetes mellitus Type 1, diabetes melittus Type 2, insulin resistance, vascular disease, skin ulcers, circulatory damage, cardiac dysfunction, diabetic nephropathy, diabetic retinopathy, microvascular disease, macrovascular disease, and diabetic neuropathy.

[00159] In certain embodiments, the compound may be used in treating a proliferative disease, e.g. tumorigenesis. In some embodiments, the the compound may be used for treating cancer. Examples of cancers treated with compounds include, but are not limited to, tumors of the breast; biliary tract; bladder; bone; brain, including glioblastomas and medulloblastomas; central and peripheral nervous system; cervix; colon; connective tissue; endocrine glands (e.g., thyroid and adrenal cortex); esophagus; endometrium; germ cells; gastrointestinal tract; head and neck; kidney; liver; lung; larynx and hypopharynx; mesothelioma; muscle; ovary, including those arising from epithelial cells, stromal cells, germ cells and mesenchymal cells; pancreas; prostate; rectum; renal, including adenocarcinoma and Wilms tumor; small intestine; soft tissue; testis, including germinal tumors such as seminoma, non-seminoma (teratomas,

choriocarcinomas), stromal tumors, and germ cell tumors; thyroid, including thyroid

adenocarcinoma and medullar carcinoma; stomach; skin, including melanoma, Kaposi's sarcoma, basocellular cancer, and squamous cell cancer; ureter; vagina; and vulva;

retinoblastoma; leukemia and lymphoma, namely non-Hodgkins disease, lymphocytic lymphomas, chronic and acute myeloid leukemia (CML/AML), acute lymphoblastic leukemia (ALL), chronic lymphocytic leukemia (CLL), Hodgkins disease, multiple myeloma, and T-cell lymphoma; myelodysplasia syndrome; plasma cell neoplasia; paraneoplastic syndromes;

intraepithelial neoplasms including Bowen's disease and Paget' s disease; neuroblastomas; oral cancer including squamous cell carcinoma; sarcomas including leiomyosarcoma,

rhabdomyosarcoma, liposarcoma, fibrosarcoma, and osteosarcoma; cancers of unknown primary site; and AIDS-related malignancies. Other cancers will be known to one of ordinary skill in the art.

[00160] In certain embodiments, the compound may be used for treating or lessening the severity of autoimmune diseases including, but not limited to, inflammatory bowel disease, arthritis, systemic lupus erythematosus, rheumatoid arthritis, psoriatic arthritis, osteoarthritis, Still's disease, juvenile arthritis, diabetes, myasthenia gravis, Hashimoto's thyroiditis, Ord's thyroiditis, Graves' disease, Sjogren's syndrome, multiple sclerosis, Guillain-Barre syndrome, acute disseminated encephalomyelitis, Addison's disease, opsoclonus-myoclonus syndrome, ankylosing spondylosis, antiphospholipid antibody syndrome, aplastic anemia, autoimmune hepatitis, celiac disease, Goodpasture's syndrome, idiopathic thrombocytopenic purpura, optic neuritis, scleroderma, primary biliary cirrhosis, Reiter' s syndrome, Takayasu' s arteritis, temporal arteritis, warm autoimmune hemolytic anemia, Wegener's granulomatosis, psoriasis, alopecia universalis, Behcet's disease, chronic fatigue, dysautonomia, endometriosis, interstitial cystitis, neuromyotonia, scleroderma, or vulvodynia.

[00161] In some embodiments, the compound may be used for treating or lessening the severity of one or more diseases and conditions, wherein the disease or condition is selected from immune-related conditions or diseases, which include, but are not limited to graft versus host disease, transplantation, transfusion, anaphylaxis, allergies (e.g., allergies to plant pollens, latex, drugs, foods, insect poisons, animal hair, animal dander, dust mites, or cockroach calyx), type I hypersensitivity, allergic conjunctivitis, allergic rhinitis, and atopic dermatitis.

[00162] In some embodiments, the compound may be used for treating or lessening the severity of an inflammatory disease including, but not limited to, asthma, appendicitis, Blau syndrome, blepharitis, bronchiolitis, bronchitis, bursitis, cervicitis, cholangitis, cholecystitis, chronic obstructive pulmonary disease (COPD), chronic recurrent multifocal osteomyelitis (CRMO), colitis, conjunctivitis, cryopyrin associated periodic syndrome (CAPS), cystitis, dacryoadenitis, dermatitis, dermatomyositis, dry eye syndrome, encephalitis, endocarditis, endometritis, enteritis, enterocolitis, epicondylitis, epididymitis, familial cold-induced autoinflammatory syndrome, familial Mediterranean fever (FMF), fasciitis, fibrositis, gastritis, gastroenteritis, hepatitis, hidradenitis suppurativa, laryngitis, mastitis, meningitis, mevalonate kinase deficiency (MKD), Muckle-Well syndrome, myelitis myocarditis, myositis, nephritis, oophoritis, orchitis, osteitis, inflammatory osteolysis, otitis, pancreatitis, parotitis, pericarditis, peritonitis, pharyngitis, pleuritis, phlebitis, pneumonitis, pneumonia, proctitis, prostatitis, pulmonary fibrosis, pyelonephritis, pyoderma gangrenosum and acne syndrome (PAPA), pyogenic sterile arthritis, rhinitis, salpingitis, sinusitis, stomatitis, synovitis, systemic juvenile rheumatoid arthritis, tendonitis, TNF receptor associated periodic syndrome (TRAPS), tonsillitis, undifferentiated spondyloarthropathy, undifferentiated arthropathy, uveitis, vaginitis, vasculitis, vulvitis, chronic inflammation resulting from chronic viral or bacteria infections, or psoriasis (e.g., plaque psoriasis, pustular psoriasis, erythrodermic psoriasis, guttate psoriasis or inverse psoriasis).

[00163] In certain embodiments, the compound may be used for treating or lessening the severity of arthropathies and osteopathological diseases including, but not limited to, rheumatoid arthritis, osteoarthrtis, gout, polyarthritis, and psoriatic arthritis.

[00164] In certain embodiments, the compound may be used for treating or lessening the severity of acute and chronic inflammatory diseases including, but not limited to, ulcerative colitis, inflammatory bowel disease, Crohn's disease, dry eye syndrome, allergic rhinitis, allergic dermatitis, cystic fibrosis, chronic obstructive bronchitis, and asthma.

[00165] In certain embodiments, the compound may be used for treating or lessening the severity of hyperproliferative diseases including, but not limited to, psoriasis or smooth muscle cell proliferation including vascular proliferative disorders, atherosclerosis, and restenosis. In certain embodiments, the compounds may be used for treating or lessening the severity of endometriosis, uterine fibroids, endometrial hyperplasia, and benign prostate hyperplasia.

[00166] In certain embodiments, the compounds may be used for treating or lessening the severity of neurodegenerative disorders and/or tauopathies including, but not limited to,

Alzheimer's disease, progressive supranuclear palsy, corticobasal degeneration, frontotemporal lobar degeneration, Pick' s disease, Parkinson's disease, Lewy body disease, or amyotropic lateral sclerosis (ALS).

[00167] Provided herein are methods for the treatment of mammals, including humans, which are suffering from one of the above-mentioned conditions, illnesses, disorders, or diseases. The methods comprise that a therapeutically effective amount of one or more of the identified compounds or pharmaceutically acceptable compositions thereof is administered to the subject in need of such treatment.

[00168] The invention further includes methods for inhibiting OGT in a cell or tissue using an identified compound.

[00169] The invention further relates to the use of the identified compound for the production of pharmaceutical compositions which are employed for the treatment and/or prophylaxis and/or amelioration of the diseases, disorders, illnesses, and/or conditions as mentioned herein.

[00170] The invention further relates to the use of an identified compound for the production of pharmaceutical compositions that modulate (e.g. inhibit) OGT activity.

[00171] The invention further relates to the use of an identified compound for the production of pharmaceutical compositions which can be used for treating, preventing, or ameliorating diseases responsive to inhibiting OGT, such as diabetes and complications thereof, neurodegenerative diseases, cancers, autoimmune diseases, and inflammatory diseases, such as any of those diseases mentioned herein.

[00172] The therapeutically effective amount of the compound or pharmaceutical composition thereof will vary from subject to subject, depending on the species, age, and general condition of the subject, the particular compound, its mode of administration, its mode of activity, and the like. The compounds are typically formulated in dosage unit form for ease of administration and uniformity of dosage. It will be understood, however, that the total daily usage of the compounds and compositions will be decided by the attending physician within the scope of sound medical judgment. The specific therapeutically effective dose level for any particular patient or organism will depend upon a variety of factors including the disorder being treated and the severity of the disorder; the activity of the specific compound employed; the specific composition employed; the age, body weight, general health, sex, and diet of the patient; the time of administration, route of administration, and rate of excretion of the specific compound employed; the duration of the treatment; drugs used in combination or coincidental with the specific compound employed; and like factors well known in the medical arts.

[00173] Furthermore, after formulation with an appropriate pharmaceutically acceptable excipient in a desired dosage, the pharmaceutical compositions can be administered to humans and other animals orally, rectally, parenterally, intracisternally, intravaginally, intraperitoneally, topically (as by powders, ointments, or drops), bucally, as an oral or nasal spray, or the like. In certain embodiments, the compound is administered orally or parenterally at dosage levels sufficient to deliver from about 0.001 mg/kg to about 100 mg/kg, from about 0.01 mg/kg to about 50 mg/kg, from about 0.1 mg/kg to about 40 mg/kg, from about 0.5 mg/kg to about 30 mg/kg, from about 0.01 mg/kg to about 10 mg/kg, from about 0.1 mg/kg to about 10 mg/kg, and from about 1 mg/kg to about 25 mg/kg, of subject body weight per day, one or more times a day, to obtain the desired therapeutic effect. The desired dosage may be delivered three times a day, two times a day, once a day, every other day, every third day, every week, every two weeks, every three weeks, or every four weeks. In certain embodiments, the desired dosage may be delivered using multiple administrations (e.g. , two, three, four, five, six, seven, eight, nine, ten, eleven, twelve, thirteen, fourteen, or more administrations).

[00174] Liquid dosage forms for oral and parenteral administration include, but are not limited to, pharmaceutically acceptable emulsions, microemulsions, solutions, suspensions, syrups and elixirs. In addition to the active compound, the liquid dosage forms may contain inert diluents commonly used in the art such as, for example, water or other solvents, solubilizing agents and emulsifiers such as ethyl alcohol, isopropyl alcohol, ethyl carbonate, ethyl acetate, benzyl alcohol, benzyl benzoate, propylene glycol, 1,3-butylene glycol, dimethylformamide, oils (in particular, cottonseed, groundnut, corn, germ, olive, castor, and sesame oils), glycerol, tetrahydrofurfuryl alcohol, polyethylene glycols and fatty acid esters of sorbitan, and mixtures thereof. Besides inert diluents, the oral compositions can also include adjuvants such as wetting agents, emulsifying and suspending agents, sweetening, flavoring, and perfuming agents. In certain embodiments for parenteral administration, the compound is mixed with solubilizing agents such polyethoxylated castor oil, alcohols, oils, modified oils, glycols, polysorbates, cyclodextrins, polymers, and combinations thereof.

[00175] Injectable preparations, for example, sterile injectable aqueous or oleaginous suspensions may be formulated according to the known art using suitable dispersing or wetting agents and suspending agents. The sterile injectable preparation may also be a sterile injectable solution, suspension or emulsion in a nontoxic parenterally acceptable diluent or solvent, for example, as a solution in 1,3-butanediol. Among the acceptable vehicles and solvents that may be employed are water, Ringer's solution, U.S.P. and isotonic sodium chloride solution. In addition, sterile, fixed oils are conventionally employed as a solvent or suspending medium. For this purpose any bland fixed oil can be employed including synthetic mono- or diglycerides. In addition, fatty acids such as oleic acid are used in the preparation of injectables.

[00176] The injectable formulations can be sterilized, for example, by filtration through a bacterial -retaining filter, or by incorporating sterilizing agents in the form of sterile solid compositions which can be dissolved or dispersed in sterile water or other sterile injectable medium prior to use.

[00177] In order to prolong the effect of a compound, it is often desirable to slow the absorption of the drug from subcutaneous or intramuscular injection. This may be accomplished by the use of a liquid suspension of crystalline or amorphous material with poor water solubility. The rate of absorption of the drug then depends upon its rate of dissolution which, in turn, may depend upon crystal size and crystalline form. Alternatively, delayed absorption of a

parenterally administered drug form is accomplished by dissolving or suspending the drug in an oil vehicle. Injectable depot forms are made by forming microencapsule matrices of the drug in biodegradable polymers such as poly(lactide-co-glycolide). Depending upon the ratio of drug to polymer and the nature of the particular polymer employed, the rate of drug release can be controlled. Examples of other biodegradable polymers include poly(orthoesters) and

poly(anhydrides). Depot injectable formulations are also prepared by entrapping the drug in liposomes or microemulsions which are compatible with body tissues.

[00178] Compositions for rectal or vaginal administration are preferably suppositories which can be prepared by mixing the compound with suitable non-irritating excipients or carriers such as cocoa butter, polyethylene glycol or a suppository wax which are solid at ambient temperature but liquid at body temperature and therefore melt in the rectum or vaginal cavity and release the active compound.

[00179] Solid dosage forms for oral administration include capsules, tablets, pills, powders, and granules. In such solid dosage forms, the active compound is mixed with at least one inert, pharmaceutically acceptable excipient or carrier such as sodium citrate or dicalcium phosphate and/or a) fillers or extenders such as starches, lactose, sucrose, glucose, mannitol, and silicic acid, b) binders such as, for example, carboxymethylcellulose, alginates, gelatin, polyvinylpyrrolidinone, sucrose, and acacia, c) humectants such as glycerol, d) disintegrating agents such as agar-agar, calcium carbonate, potato or tapioca starch, alginic acid, certain silicates, and sodium carbonate, e) solution retarding agents such as paraffin, f) absorption accelerators such as quaternary ammonium compounds, g) wetting agents such as, for example, cetyl alcohol and glycerol monostearate, h) absorbents such as kaolin and bentonite clay, and i) lubricants such as talc, calcium stearate, magnesium stearate, solid polyethylene glycols, sodium lauryl sulfate, and mixtures thereof. In the case of capsules, tablets and pills, the dosage form may also comprise buffering agents.

[00180] Solid compositions of a similar type may also be employed as fillers in soft and hard-filled gelatin capsules using such excipients as lactose or milk sugar as well as high molecular weight polyethylene glycols and the like. The solid dosage forms of tablets, dragees, capsules, pills, and granules can be prepared with coatings and shells such as enteric coatings and other coatings well known in the pharmaceutical formulating art. They may optionally contain opacifying agents and can also be of a composition that they release the active ingredient(s) only, or preferentially, in a certain part of the intestinal tract, optionally, in a delayed manner. Examples of embedding compositions which can be used include polymeric substances and waxes. Solid compositions of a similar type may also be employed as fillers in soft and hard-filled gelatin capsules using such excipients as lactose or milk sugar as well as high molecular weight polyethylene glycols and the like.

[00181] The active compound can also be in micro-encapsulated form with one or more excipients as noted above. The solid dosage forms of tablets, dragees, capsules, pills, and granules can be prepared with coatings and shells such as enteric coatings, release controlling coatings and other coatings well known in the pharmaceutical formulating art. In such solid dosage forms the active protein may be admixed with at least one inert diluent such as sucrose, lactose or starch. Such dosage forms may also comprise, as is normal practice, additional substances other than inert diluents, e.g., tableting lubricants and other tableting aids such a magnesium stearate and microcrystalline cellulose. In the case of capsules, tablets, and pills, the dosage forms may also comprise buffering agents. They may optionally contain opacifying agents and can also be of a composition that they release the active ingredient(s) only, or preferentially, in a certain part of the intestinal tract, optionally, in a delayed manner. Examples of embedding compositions which can be used include polymeric substances and waxes.

[00182] Formulations suitable for topical administration include liquid or semi-liquid preparations such as liniments, lotions, gels, applicants, oil-in- water or water-in-oil emulsions such as creams, ointments, or pastes; or solutions or suspensions such as drops. Formulations for topical administration to the skin surface can be prepared by dispersing the compound with a dermatologically acceptable carrier such as a lotion, cream, ointment, or soap. Useful carriers are capable of forming a film or layer over the skin to localize application and inhibit removal. For topical administration to internal tissue surfaces, the compound can be dispersed in a liquid tissue adhesive or other substance known to enhance adsorption to a tissue surface. For example, hydroxypropylcellulose or fibrinogen/thrombin solutions can be used to advantage.

Alternatively, tissue-coating solutions such as pectin-containing formulations can be used.

Ophthalmic formulation, ear drops, and eye drops are also contemplated as being within the scope of this invention. Additionally, the present invention contemplates the use of transdermal patches, which have the added advantage of providing controlled delivery of a compound to the body. Such dosage forms can be made by dissolving or dispensing the compound in the proper medium. Absorption enhancers can also be used to increase the flux of the compound across the skin. The rate can be controlled by either providing a rate controlling membrane or by dispersing the compound in a polymer matrix or gel.

[00183] Additionally, the carrier for a topical formulation can be in the form of a hydroalcoholic system (e.g., liquids and gels), an anhydrous oil or silicone based system, or an emulsion system, including, but not limited to, oil-in- water, water-in-oil, water-in- oil-in- water, and oil-in-water-in-silicone emulsions. The emulsions can cover a broad range of consistencies including thin lotions (which can also be suitable for spray or aerosol delivery), creamy lotions, light creams, heavy creams, and the like. The emulsions can also include microemulsion systems. Other suitable topical carriers include anhydrous solids and semisolids (such as gels and sticks); and aqueous based mousse systems.

[00184] It will also be appreciated that the compound and pharmaceutical compositions thereof can be employed in combination therapies, that is, the compound and pharmaceutical compositions can be administered concurrently with, prior to, or subsequent to, one or more other desired therapeutics or medical procedures. The particular combination of therapies (therapeutics or procedures) to employ in a combination regimen will take into account compatibility of the desired therapeutics and/or procedures and the desired therapeutic effect to be achieved. It will also be appreciated that the therapies employed may achieve a desired effect for the same disorder (for example, an inventive compound may be administered concurrently with another anticancer agent), or they may achieve different effects (e.g., control of any adverse effects).

[00185] A compound or pharmaceutical compositions thereof may be provided as a pharmaceutical pack or kit comprising one or more containers filled with one or more of the ingredients of the pharmaceutical compositions, and in certain embodiments, includes an additional approved therapeutic agent for use as a combination therapy. Optionally associated with such container(s) can be a notice in the form prescribed by a governmental agency regulating the manufacture, use, or sale of pharmaceutical products, which notice reflects approval by the agency of manufacture, use or sale for human administration.

[00186] These and other aspects of the present invention will be further appreciated upon consideration of the following Examples, which are intended to illustrate certain particular embodiments of the invention but are not intended to limit its scope, as defined by the claims.

EXAMPLES

[00187] The present invention will be more specifically illustrated by the following examples. However, it should be understood that the present invention is not limited by these examples in any manner.

Example 1

[00188] It has been suggested that strategies to reduce OGT activity may have therapeutic value for treating diabetic complications, cancer, and other diseases.15 The lack of a crystal structure has been a major impediment to developing inhibitors, to understanding substrate recognition, and to exploring OGT's molecular mechanisms. OGT comprises two distinct regions: an N-terminal region consisting of a series of tetratricopeptide repeat (TPR) units 21 ' 22 and a multidomain catalytic region (Figure la). The TPR domain is proposed to scaffold interactions with other proteins and may play a role in determining selectivity. 23 A crystal structure comprising 11.5 TPR units of human OGT was reported in 2004, 23 but there have been no structures of the catalytic region. Based on sequence analysis combined with structures of bacterial glycosyltransferases, 24-"28 including a homologous bacterial protein of unknown function, 27 ' 28 the catalytic region was predicted to belong to the GT-B superfamily of

glycosyltransferases (Gtfs). Members of this superfamily glycosylate a wide variety of molecules, but OGT is the only member known to glycosylate polypeptides. OGT is also atypical because it contains an uncharacterized intervening sequence (-120 amino acids) in the middle of the catalytic region. In addition, OGT is proposed to contain a phosphatidylinositol (3,4,5)-trisphosphate (PIP3) binding site that is involved in recruiting the enzyme to membranes in response to insulin receptor activation.10 The structures described here reveal how OGT recognizes peptide substrates, provide information on the catalytic mechanism, and show the fold of the intervening domain which forms a large basic patch on the surface of the protein.

[00189] The structures described herein are of an active human OGT construct (I1OGT4.5) containing 4.5 TPR units. This construct has similar catalytic properties as the full-length enzyme (Figs. 4 and 5) 30. One crystal structure (2.8 A 0 ) is a complex with UDP (referred to as

OGT- UDP); the other structure (1.95 A) is a complex containing UDP and a well-characterized peptide substrate, the CKII peptide 30 (referred to as OGT-UDP-peptide, Table 1). Since the first two TPR units in the crystallized hOGT4 5 constructs overlap with the last two TPR units of the previously crystallized TPR domain, complete structures for these complexes of human OGT can be assembled.

[00190] The overall fold of the OGT-UDP complex is shown in Figure lb. The catalytic region contains three domains: the N-terminal domain (N-Cat), the C-terminal domain (C-Cat), and an intervening domain (Int-D). The N-Cat and C-Cat domains have Rossmann-like folds typical of GT-B superfamily members; however, the N-Cat domain is distinctive in containing two additional helices (HI and H2) that form an essential part of the active site (Figure lb). The intervening sequence folds into a novel domain that packs exclusively against the C-Cat domain, ° 2

occluding 517 A of its surface. The UDP moiety binds in a pocket in the C-Cat domain near the interface with the N-Cat domain . This pocket is lined with conserved residues shown to be important for catalytic activity (Figure 2b and Table 3). A transitional helix (H3) links the catalytic region to the TPR repeats, which spiral along the upper surface of the catalytic region from the C-Cat domain to the N-Cat domain (Figure 1). The first two TPR repeats of the I1OGT4.5 construct (corresponding to TPRs 10 and 11 of ncOGT) make several contacts with the long N-terminal helix of the N-Cat domain (helix H2 in Figure lb), with the result that the TPR domain caps the top of the catalytic region (Figure lc). The TPRs and the catalytic region are demarcated by a narrow horizontal cleft.

[00191] The OGT-UDP-peptide complex, which crystallized in a different space group from the OGT-UDP complex, has a wider cleft between the TPR domain and the catalytic region than the OGT-UDP complex (Figure lc and Figure 2a). Opening of the cleft is due to a hinge- o

like movement between TPRs 12 and 13, which results in a 6 A shift of TPR 10 away from the catalytic domain compared with the OGT-UDP structure (Figure 6). This movement allows the peptide to fit in the cleft. Based on the structure of this complex, we propose that protein substrates enter the active site through the cleft between the catalytic region and the TPR domain, with the TPR domain regulating access. Since the TPR units have considerable

23

flexibility relative to one another , the cleft may open wider to accommodate larger protein substrates, and interactions with other proteins that induce or stabilize an open cleft conformation may play a role in substrate selection.

[00192] The CKII peptide binds in the cleft between the TPR domain and the catalytic region, at the interface between the N-Cat and C-Cat domains (Fig. 2a and b, Table 3). This peptide, YPGGSTPVSSANMM30 (SEQ ID NO: l), contains three serines and a threonine, but only one serine (underlined) is glycosylated by OGT. The side chain of this serine points directly into the nucleotide-sugar binding site near the predicted location of the anomeric carbon of the GlcNAc sugar (Fig. 2c and Fig. 7). The two residues N-terminal to the reactive serine lie directly over the UDP moiety; the residues C-terminal to the serine traverse towards the back of the cleft along the long N-terminal helix (H2) that forms the top of the N-Cat domain. OGT glycosylates a wide range of target peptides, but it displays clear preferences for sequences in which the residues flanking the glycosylated amino acid enforce an extended conformation (e.g., prolines and β-branched amino acids; Fig. 8 and Table 4). Consistent with these preferences, the peptide is anchored mainly by contacts from OGT side chains to the amide backbone, with an additional backbone contact from the bound UDP moiety to the amide of the serine that gets glycosylated. The cleft is densely filled with ordered water molecules, which may enable OGT to recognize peptides containing a range of charged and uncharged sidechains. Since the peptide is anchored by a set of backbone contacts, it is reasonable to infer that protein substrates are glycosylated on flexible regions such as loops or termini that have accessible backbones and can bind in an extended conformation.

[00193] The closed conformation of the substrate-binding cleft in the OGT-UDP structure is stabilized by a 'latch' comprising contacts between TPRs 10/11 and the H2 helix of the catalytic domain (Figure 2a and Figure 6). Opening of the cleft in the OGT-UDP-peptide complex occurs due to a hinge-like motion around a pivot point between TPRs 12 and 13. The two structures suggest that glycosylation substrates enter the active site from the face of the enzyme shown in Fig. 2a, with the TPR domain restricting or allowing access depending on its conformation and its interactions with the catalytic domain. Molecular dynamics simulations indicate that the 'hinge' between the catalytic domain and the TPR domain is capable of large motions that fully expose the active site, which would allow protein substrates to approach closely enough for surface loops to enter. The molecular mechanisms that facilitate or stabilize opening of the cleft to allow access of protein substrates may involve interactions between protein substrates or adapter proteins and the other regions of OGT.

[00194] The OGT-UDP-peptide complex, in addition to revealing how peptide substrates bind, provides new insights into the kinetic mechanism. OGT was previously shown to have a sequential mechanism and it was suggested that the substrates bind in a random order, but no experiments addressing reaction order have been reported. Since the peptide substrate binds directly over the nucleotide-sugar binding pocket, blocking access to it, the OGT-UDP-peptide structure strongly suggests that the kinetic mechanism is ordered with UDP-GlcNAc binding first (Figure 2b). This kinetic mechanism is consistent with the contact from the a-phosphate of the UDP moiety to the backbone amide of the reactive serine residue (Figure 2c), which suggests that bound UDP-GlcNAc helps orient the peptide substrate for glycosylation. An ordered mechanism could also explain the observation that we were able to obtain crystals of the OGT- UDP complex and the OGT-UDP-peptide complex, but not of an OGT-peptide complex. Since the structure suggests an ordered bi bi mechanism in which UDP-GlcNAc binds first, but a random mechanism was previously proposed, we evaluated the mode of inhibition for UDP- GlcNAc by UDP to distinguish between these possibilities. The competitive inhibition pattern observed at saturating peptide concentrations is consistent with an ordered, but not a random, mechanism, Figure 5.

[00195] Another insight from the crystal structure is the identity of the catalytic base.

Based on analyses of other GT-B family members, including the bacterial OGT homolog, it was proposed that His558 is the catalytic base. Although it was verified that this residue is critical for catalytic activity, the peptide complex shows that it is more than 5 A away from the reactive serine hydroxyl and makes an apparent hydrogen bond with the backbone carbonyl of the preceding residue. In contrast, His498, which is invariant in metazoan OGTs but absent in the homologous bacterial enzyme, protrudes from helix HI into the active site within 3.5 A of the Ser* hydroxyl. Since His498 is critical for activity and is located between the reactive serine hydroxyl and the GlcNAc binding pocket, it is the probable catalytic base in OGT.

[00196] Computational methods were used to dock UDP-GlcNAc into the active site of the UDP complex. In its most preferred binding mode, the UDP-GlcNAc is oriented with the β face of the sugar exposed and the anomeric carbon aligned with the reactive serine of the peptide. This UDP-GlcNAc conformation is consistent with experimental data suggesting that the C2 N-acetyl moiety projects out of the sugar binding pocket, and it is similar to the conformation of UDP-GlcNAc in the structure of another GT-B family member 25. Most important, it is also consistent with the enzymatic reaction, which involves displacement of the a-UDP group to yield an inverted product (Fig. 2d and Fig. 7). Based on the accumulated biochemical and structural data, we have proposed a general mechanism for the reaction, which is illustrated in Fig. 2e. In our mechanism, His498 acts as the catalytic base. This histidine, which is invariant in metazoan OGTs but absent in the homologous bacterial enzyme, is located on helix HI at the beginning of the N-Cat domain (Fig. lb). It protrudes into the active site and approaches within 3.55 A of the reactive serine. We have confirmed its importance in catalysis by mutagenesis (Fig. 2d). Displacement of the UDP moiety is facilitated by a stabilizing interaction with Lys842, which has also been shown to be essential for activity. 27 ' 28

[00197] His558 was previously proposed to be the catalytic base in OGT, and we have verified the importance of this residue in catalytic activity (Figure 2d). However, in the structure of the peptide complex, His558 is more than 5 A from the reactive serine hydroxyl (Figure 2c). It makes an apparent hydrogen bond to the backbone carbonyl of the residue preceding the reactive serine and thus may play a role in peptide binding (Figure 2c).

[00198] The unique intervening domain of OGT has a previously unobserved topology, comprising a seven- stranded β-sheet with an antiparallel/parallel/parallel repeat (Figure 3b and Figure 9). The sheet is stabilized by three a-helices, two from the intervening domain and one from the C-Cat domain, and it contains three large loops. An electrostatic surface rendering of OGT shows a very large basic patch comprising thirteen basic residues, four of which are on the helix in the C-Cat domain that contains a motif proposed to be involved in PIP3-binding (the PPO motif).10 Nine additional basic residues are in the intervening domain (Figure 3b), concentrated along an exposed edge of the β-sheet core and in the adjacent loop between β3 and β4 (Figure 3b and Figure 9). Electron density is missing for twelve residues in the β3-β4 loop and the broken ends extend over the C-Cat helix containing the proposed PPO motif.10 It is possible that this flexible region of the intervening domain somehow regulates PIP3 binding since it covers the PPO motif. Several mutants in which the Int-D domain lysines were substituted with serines were made. Additionally, the entire intervening domain was replaced with a short linker (Figure 9 and and Table 3). All mutants were catalytically active, but a role for the Int-D domain in PIP binding could not be verified. Since the intervening domain is not required for in vitro catalytic activity, it must be involved in other functions in vivo. These functions may include substrate selection, cellular localization, or interactions with regulatory factors or receptors. While the details of PIP binding remain unclear, the extensive basic patch on OGT is quite striking and is consistent with a role for the intervening domain in interacting with negatively charged membranes (Figure 3c).

References for Background, Summary, Deatailed Description, and Example 1

1. Hart, G.W., Housley, M.P. & Slawson, C. Cycling of O-linked beta-N-acetylglucosamine on nucleocytoplasmic proteins. Nature 446, 1017-22 (2007).

2. O'Donnell, N., Zachara, N.E., Hart, G.W. & Marth, J.D. Ogt-dependent X-chromosome- linked protein glycosylation is a requisite modification in somatic cell function and embryo viability. Mol Cell Biol 24, 1680-90 (2004). 3. Torres, C.R. & Hart, G.W. Topography and polypeptide distribution of terminal N- acetylglucosamine residues on the surfaces of intact lymphocytes. Evidence for O-linked GlcNAc. J Biol Chem 259, 3308-17 (1984).

4. Haltiwanger, R.S., Holt, G.D. & Hart, G.W. Enzymatic addition of O-GlcNAc to nuclear and cytoplasmic proteins. Identification of a uridine diphospho-N-acetylglucosamine:peptide beta-N-acetylglucosaminyltransferase. J Biol Chem 265, 2563-8 (1990).

5. Yang, X., Zhang, F. & Kudlow, J.E. Recruitment of O-GlcNAc transferase to promoters by corepressor mSin3A: coupling protein O-GlcNAcylation to transcriptional repression. Cell 110, 69-80 (2002).

6. Yang, W.H. et al. Modification of p53 with O-linked N-acetylglucosamine regulates p53 activity and stability. Nat Cell Biol 8, 1074-83 (2006).

7. Dias, W.B., Cheung, W.D., Wang, Z. & Hart, G.W. Regulation of calcium/calmodulin- dependent kinase IV by O-GlcNAc modification. J Biol Chem 284, 21327-37 (2009).

8. Wells, L., Kreppel, L.K., Comer, F.I., Wadzinski, B.E. & Hart, G.W. O-GlcNAc transferase is in a functional complex with protein phosphatase 1 catalytic subunits. J Biol Chem 279, 38466-70 (2004).

9. Fujiki, R. et al. GlcNAcylation of a histone methyltransferase in retinoic-acid-induced granulopoiesis. Nature 459, 455-9 (2009).

10. Yang, X. et al. Phosphoinositide signalling links O-GlcNAc transferase to insulin resistance. Nature 451, 964-9 (2008).

11. Brownlee, M. Biochemistry and molecular cell biology of diabetic complications. Nature 414, 813-20 (2001).

12. Caldwell, S.A. et al. Nutrient sensor O-GlcNAc transferase regulates breast cancer tumorigenesis through targeting of the oncogenic transcription factor FoxMl. Oncogene 29, 2831-42 (2010).

13. Liu, F., Iqbal, K., Grundke-Iqbal, I., Hart, G.W. & Gong, C.X. O-GlcNAcylation regulates phosphorylation of tau: a mechanism involved in Alzheimer's disease. Proc Natl Acad Sci U SA lOl, 10804-9 (2004).

14. Love, D.C. & Hanover, J. A. The hexosamine signaling pathway: deciphering the "O- GlcNAc code". Sci STKE 2005, rel3 (2005). 15. Dentin, R., Hedrick, S., Xie, J., Yates, J., 3rd & Montminy, M. Hepatic glucose sensing via the CREB coactivator CRTC2. Science 319, 1402-5 (2008).

16. Wells, L., Vosseller, K. & Hart, G.W. Glycosylation of nucleocytoplasmic proteins: signal transduction and O-GlcNAc. Science 291, 2376-8 (2001).

17. Gambetta, M.C., Oktaba, K. & Muller, J. Essential role of the glycosyltransferase sxc/Ogt in polycomb repression. Science 325, 93-6 (2009).

18. Sinclair, D.A. et al. Drosophila O-GlcNAc transferase (OGT) is encoded by the

Polycomb group (PcG) gene, super sex combs (sxc). Proc Natl Acad Sci U S A 106, 13427-32 (2009).

19. Love, D.C. et al. Dynamic O-GlcNAc cycling at promoters of Caenorhabditis elegans genes regulating longevity, stress, and immunity. Proc Natl Acad Sci U S A 107, 7413-8 (2010).

20. Goldberg, H.J., Whiteside, C.I., Hart, G.W. & Fantus, I.G. Posttranslational, reversible O-glycosylation is stimulated by high glucose and mediates plasminogen activator inhibitor- 1 gene expression and Spl transcriptional activity in glomerular mesangial cells. Endocrinology 147, 222-31 (2006).

21. Kreppel, L.K., Blomberg, M.A. & Hart, G.W. Dynamic glycosylation of nuclear and cytosolic proteins. Cloning and characterization of a unique O-GlcNAc transferase with multiple tetratricopeptide repeats. J Biol Chem 272, 9308-15 (1997).

22. Lubas, W.A., Frank, D.W., Krause, M. & Hanover, J.A. O-Linked GlcNAc transferase is a conserved nucleocytoplasmic protein containing tetratricopeptide repeats. / Biol Chem 272, 9316-24 (1997).

23. Jinek, M. et al. The superhelical TPR-repeat domain of O-linked GlcNAc transferase exhibits structural similarities to importin alpha. Nat Struct Mol Biol 11, 1001-7 (2004).

24. Ha, S., Walker, D., Shi, Y. & Walker, S. The 1.9 A crystal structure of Escherichia coli MurG, a membrane- associated glycosyltransferase involved in peptidoglycan biosynthesis.

Protein Sci 9, 1045-52 (2000).

25. Hu, Y. et al. Crystal structure of the MurG:UDP-GlcNAc complex reveals common structural principles of a superfamily of glycosyltransferases. Proc Natl Acad Sci U S A 100, 845-9 (2003).

26. Wrabl, J.O. & Grishin, N.V. Homology between O-linked GlcNAc transferases and proteins of the glycogen phosphorylase superfamily. J Mol Biol 314, 365-74 (2001). 27. Martinez-Fleites, C. et al. Structure of an O-GlcNAc transferase homolog provides insight into intracellular glycosylation. Nat Struct Mol Biol 15, 764-5 (2008).

28. Clarke, A.J. et al. Structural insights into mechanism and specificity of O-GlcNAc transferase. Embo J ll, 2780-8 (2008).

29. Lairson, L.L., Henrissat, B., Davies, G.J. & Withers, S.G. Glycosyltransferases:

structures, functions, and mechanisms. Annu Rev Biochem 77, 521-55 (2008).

30. Kreppel, L.K. & Hart, G.W. Regulation of a cytosolic and nuclear O-GlcNAc transferase. Role of the tetratricopeptide repeats. J Biol Chem 214, 32015-22 (1999).

Methods

[00199] Protein purification. After optimizing the construct and protein expression, human OGT (amino acids 313-1031) was expressed in E .coli in a modified pET24b vector (Novagen) with a T7 tag and 8 His tag followed by an HRV3C protease cleavage site

(LEVLFQGP, SEQ ID NO: 56) at the N-terminus. The plasmid was transformed into

BL21(DE3) cells. Cultures were grown at 37 °C after diluting an overnight culture 1 to 100 in fresh LB media. Cells were grown to an OD6oo of 1.1, at which point they were transferred to 16 °C. After letting the cells grow at 16 °C for 30 minutes, they were induced with 0.2 mM IPTG and grown overnight at 16 °C for 16 hours. Cells were then pelleted and resuspended in TBS (20 mM Tris, pH 7.4, 250 mM NaCl) and supplemented with 1 mM PMSF and 0.1 mg/ml lysozyme. The cells were lysed and the lysate was centrifuged at 5,000 x g for 20 minutes to remove unbroken cells. The supernatant was then centrifuged at 37,000 rpm to further clean the lysate. Imidazole was then added to the supernatant to a final concentration of 40 mM before the lysate was incubated with Ni-NTA agarose superflow resin (Qiagen) which was pre- washed with TBS + 40 mM imidazole for batch nickel affinity purification. After incubating the lysate and the resin with gentle rocking at 4 °C, the flow through was removed and the resin was washed with 10 column volumes of TBS + 50 mM imidazole. The protein was then eluted with 4 column volumes of TBS + 250 mM imidazole. The eluate was then supplemented with 0.5 μΜ

Tris(hydroxypropyl)phosphine (THP) to prevent aggregation and then concentrated with centrifugal concentrators (Millipore, Billerica, MA). After protein concentration determination, the N terminal tags were cleaved by adding HRV 3C protease (EMD) to the concentrated purified protein at a ratio 1 unit/150 μg of protein and incubating at 4 °C for 16 hours. Following cleavage, the protein was further purified by gel filtration on a Superdex 200 column (GE Healthcare) in TBS (20 mM Tris, pH 8.0, 150 mM NaCl) + 0.5 μΜ THP (EMD). The fractions were collected and concentrated using centrifugal concentrators again. The hOGT4 5 protein was monomeric in solution, as determined by gel filtration and analytical ultracentrifugation. The protein was then diluted 1: 1 in water prior to setting up crystals.

[00200] Native crystals. All crystals were grown with the hanging drop method at room temperature. For the UDP structure, 7 mg/ml protein was incubated with 1 mM UDP for several hours at 4 °C. After screening, optimal crystals were obtained when 10 μΐ of protein was then mixed with 5 μΐ of reservoir solution containing 1.45 M potassium phosphate dibasic, 8 mM EDTA, and 1% xylitol. After several days, hexagonal rod crystals grew, to a maximum size of about 400 x 100 x 100 microns. Crystals were flash frozen using a cryoprotectant consisting of 1.8 M Potassium Phosphate and 27% xylitol. For the peptide-UDP complex, OGT was incubated with 1 mM UDP and 2 mM CKII3K peptide 1 ' 2 for several hours at 4 °C. Crystals were obtained by mixing 8 μΐ protein solution with 4 μΐ reservoir containing 1.6 M Li2S04 and 0.1M Bis Tris Propane, (pH 7). Trapezoidal crystals appeared after several days. Crystals were frozen in a cryprotectant consisting of 1.72 M Li2S04, 0.05 M Bis Tris Propane, pH 7.0 and 28% xylitol.

[00201] Heavy metal soaks. Several heavy metals compounds were screened using the method of Boggon and Shapiro.19 After identifying several promising heavy metal compounds, the following conditions gave useful derivatives: K2PtCl4, 10 mM, 1 hour soak; sodium aurothiomalate, 10 mM, 15 minute soak; K2PtCl4, 10 mM, 10 minute soak; K2PtBr4, 1 mM, 1 hour soak.

[00202] Data collection. All the data were collected at National Synchrotron Light Source x29 or x25 at Brookhaven National Lab except for the gold derivative, which was collected at ID24C at Advanced Photon Source at Argonne National Lab. The heavy metal derivatives were collected at the following peak wavelengths: gold at 1.0384 A and platinum at 1.0715 A. The UDP structure and all the derivatives belonged to the space group P321. The peptide complex crystals were 12. All data sets were processed with iMosflm 20 and scaled using SCALA 21.

[00203] Structure determination and refinement of the OGT-UDP structure. The structure of the native OGT-UDP complex was determined by using MIRAS with the program SHARP 22. The native data set and all the heavy atom derivative data sets were processed with iMosflm and SCALA. Heavy atom sites in the K^PtC 1 hour soak data set were first determined by using HKL2MAP . SAD phases were then obtained with the CCP4 program Phaser (Experimental Phasing). These initial phases were then used to find the heavy atom sites in the other data sets using the CCP4 25 program FFT. After obtaining all the sites, MIRAS phases to 4.4 A ° were obtained using SHARP. The figures of merit at this resolution were 0.46329 (acentric) and 0.47049 (centric). After MIRAS phasing, the map was interpretable, and we confirmed that there were four monomers in the asymmetric unit. Density modification and phase extension to 2.78 A with non-crystallographic symmetry (NCS) averaging were performed using the CCP4 program DM yielding, a map with clear side chains. A model was built using as a guide both the structure of the bacterial homologue (using a homology model generated with Swiss Model: Arnold et al. (2006) The SWISS-MODEL Workspace: A web-based environment for protein structure homology modelling, Bioinformatics 22: 195-201; Kiefer et al. (2009) The SWISS-MODEL Repository and associated resources, Nucleic Acids Research. 37:D387-D392; Peitsch, M. C. (1995) Protein modeling by E-mail, Bio/Technology 13:658-660) and the heavy atom locations. The structure was refined with CNS26. Initial rigid body refinement optimized the placement of the monomers and then the components of each monomer. After several iterative rounds of simulated annealing, individual B factor refinement, and manual adjustments using COOT 27', the UDP and waters were added, and the structure refined to an Rwork of 21% and an Rfree of 24%.

Refinement was completed in Phenix 28 using TLS refinement 29 ' 30 , minimization, and individual B factor refinement to give a final Rwork of 17.4% and Rfree of 22.3%. Figures were prepared using Pymol31 and CCP4mg32.

[00204] Structure determination and refinement of the OGT-UDP -peptide complex. Data were processed with iMosflm and Scala, and the structure was determined by molecular replacement. The refined OGT-UDP structure described above was used as a search model using the Phaser molecular replacement module 33 in CCP4. Initial molecular replacement efforts showed that while the catalytic domain was nearly identical in the UDP and UDP-Peptide co- complexes, the orientation of the TPRs relative to the catalytic domain was noticeably different. Therefore, the model was broken into three parts: the catalytic domain and two sections of the TPR domains. Using this approach, a good map and model were obtained, which confirmed the two-fold NCS present in this structure. The peptide was built by hand, as the side chains were already clear enough at this point to place the residues properly. The peptide in the crystal structure was cleaved from KKKYPGGSTPVSSANMM (SEQ ID NO: 2) to YPGGSTPVSSANMM (SEQ ID NO: 1), as confirmed by mass spectrometry. The model was then refined with Phenix. As before, repeated rounds of annealing and individual B factor refinement were interspersed with manual adjustments in COOT. Waters were then added and sulfate ions were added after refining the waters. The structure was completed with cycles of annealing, minimization, TLS and B factor refinement, leading to a final structure with Rwork of 22.4% and Rfree of 25.2%. The crystal packing for the two complexes is shown in Figure 11.

[00205] Kinetics. Point mutants were made from the full-length ncOGT using

QuickChange™ mutagenesis (Stratagene, La Jolla, CA). OGT kinetics was performed using a filter-binding assay . Briefly, reaction mixture containing 500 μΜ CKII3K peptide

(KKKYPGGSTPVSSANMM, SEQ ID NO: 2), 6 μΜ UDP-14C-GlcNAc (300 mCi/mmol specific activity), 100 nM OGT (WT or mutant protein), and buffer (125 mM NaCl, 1 mM EDTA, 20 mM potassium phosphate, pH=7.4, and 500 μΜ tris(hydroxypropyl)phosphine) were incubated at room temperature for 30 minutes. Reactions were then quenched by spotting onto Whatman P81 phosphocellulose discs (Whatman, Florham Park, NJ), washed three times for five minutes in 0.5% phosphoric acid, and counted by liquid scintillation counting. All of the reactions had <10% conversion under these conditions. Positive and negative controls were conducted similarly without enzyme, and positive controls were detected by liquid scintillation counting without phosphoric acid wash step. Reactions were allowed to proceed for either 30 minutes or 60 minutes. Data were analyzed based on triplicate experiments with linear regression using GraphPad Prism5.

[00206] Crystal Construct. The construct contains residues 313-1031 of the full-length ncOGT protein. The codon-optimized DNA sequence of the construct is shown below , from a pET24b vector. The start site is underlined, the HRV3C cleavage sequence is shown in bold and the terminator codon is shown in italics.

TAAGAAGGAGATATACATATGGCTAGCATGACTGGTGGACAGCAAATGGGTCGGGATCCGCACC ATCACCATCACCATCACCACCTGGAAGTTTTGTTCCAAGGTCCGGGT TCT TGCCCGACCCACGC

TGACTCTCTGAACAACCTGGCTAACATCAAACGTGAACAGGGTAACATCGAAGAAGCTGT TCGT CTGTACCGTAAAGCTCTGGAAGT T T TCCCGGAAT TCGCTGCTGCTCACTCTAACCTGGCT TCTG T TCTGCAGCAGCAGGGTAAACTGCAGGAAGCTCTGATGCACTACAAAGAAGCTATCCGTATCTC TCCGACCT TCGCTGACGCT TACTCTAACATGGGTAACACCCTGAAAGAAATGCAGGACGT TCAG GGTGCTCTGCAGTGCTACACCCGTGCTATCCAGATCAACCCGGCT T TCGCTGACGCTCACTCTA ACCTGGCT TCTATCCACAAAGACTCTGGTAACATCCCGGAAGCTATCGCT TCT TACCGTACCGC TCTGAAACTGAAACCGGACT TCCCGGACGCCTACTGCAACCTGGCTCACTGCCTGCAGATCGT T TGCGACTGGACCGACTACGACGAACGTATGAAAAAACTGGT T TCTATCGT TGCTGACCAGCTGG AAAAAAACCGTCTGCCGTCTGTTCACCCGCACCACTCTATGCTGTACCCGCTGTCTCACGGTTT CCGTAAAGCTATCGCTGAACGTCACGGTAACCTGTGCCTGGACAAAATCAACGTTCTGCACAAA CCGCCGTACGAACACCCGAAAGACCTGAAACTGTCTGACGGTCGTCTGCGTGTTGGTTACGTTT CTTCTGACTTCGGTAACCACCCGACCTCTCACCTGATGCAGTCTATCCCGGGTATGCACAACCC GGACAAATTCGAAGTTTTCTGCTACGCTCTGTCTCCGGACGACGGTACCAACTTCCGTGTTAAA GTTATGGCTGAAGCTAACCACTTCATCGACCTGTCTCAGATCCCGTGCAACGGTAAAGCTGCTG ACCGTATCCACCAGGACGGTATCCACATCCTGGTTAACATGAACGGTTACACCAAAGGTGCTCG TAACGAACTGTTCGCTCTGCGTCCGGCTCCGATTCAGGCTATGTGGCTGGGTTACCCGGGTACC TCTGGTGCTCTGTTCATGGACTACATCATCACCGACCAGGAAACCTCTCCGGCTGAAGTTGCTG AACAGTACTCTGAAAAACTGGCTTACATGCCGCACACCTTCTTCATCGGTGACCACGCTAACAT GTTCCCGCACCTGAAAAAAAAAGCTGTTATCGACTTCAAATCTAACGGTCACATCTACGACAAC CGTATCGTTCTGAACGGTATCGACCTGAAAGCTTTCCTGGACTCTCTGCCGGACGTTAAAATCG TTAAAATGAAATGCCCGGACGGCGGTGACAACGCTGACTCTTCTAACACCGCTCTGAACATGCC GGTTATCCCGATGAACACCATCGCTGAAGCTGTTATCGAAATGATCAACCGTGGTCAGATCCAG ATCACCATCAACGGTTTCTCTATCTCTAACGGTCTGGCTACCACCCAGATCAACAACAAAGCTG CTACCGGTGAAGAAGTTCCGCGTACCATCATCGTTACCACCCGTTCTCAGTACGGTCTGCCGGA AGACGCTATCGTTTACTGCAACTTCAACCAGCTGTACAAAATCGACCCGTCTACCCTGCAGATG TGGGCTAACATCCTGAAACGTGTTCCGAACTCTGTTCTGTGGCTGCTGCGTTTCCCGGCTGTTG GTGAACCGAACATCCAGCAGTACGCTCAGAACATGGGTCTGCCGCAGAACCGTATCATCTTCTC TCCGGTTGCTCCGAAAGAAGAACACGTTCGTCGTGGTCAGCTGGCTGACGTTTGCCTGGACACC CCGCTGTGCAACGGTCACACCACCGGTATGGACGTTCTGTGGGCTGGTACCCCGATGGTTACCA TGCCGGGTGAAACCCTGGCTTCTCGTGTTGCTGCTTCTCAGCTGACCTGCCTGGGTTGCCTGGA ACTGATCGCTAAAAACCGTCAGGAATACGAAGACATCGCTGTTAAACTGGGTACCGACCTGGAA TACCTGAAAAAAGTTCGTGGTAAAGTTTGGAAACAGCGTATCTCCTCTCCGCTGTTCAACACCA AACAGTACACCATGGAACTGGAACGTCTGTACCTGCAGATGTGGGAACACTACGCTGCTGGTAA CAAACCGGACCACATGATTAAACCGGTTGAATAACACCACCACCACCACCACCACCACTAATTG ATTAATACCTAGGCTGCTAAAC (SEQ ID NO: 3)

References for Methods

1. Kreppel, L.K. & Hart, G.W. Regulation of a cytosolic and nuclear O-GlcNAc transferase. Role of the tetratricopeptide repeats. J Biol Chem 274, 32015-22 (1999).

2. Gross, B.J., Kraybill, B.C. & Walker, S. Discovery of O-GlcNAc transferase inhibitors. J Am Chem Soc 127, 14588-9 (2005).

3. Schrodinger Software Suite. (Schrodinger LLC, New York, 2006).

4. Clarke, A.J. et al. Structural insights into mechanism and specificity of O-GlcNAc transferase EmboJll, 2780-8 (2008).

5. Gorodkin, J., Heyer, L.J., Brunak, S. & Stormo, G.D. Displaying the information contents of structural RNA alignments: the structure logos. Comput Appl Biosci 13, 583-6 (1997).

6. Schneider, T.D. & Stephens, R.M. Sequence logos: a new way to display consensus sequences. Nucleic Acids Res 18, 6097-100 (1990). 7. Lazarus, B.D., Roos, M.D. & Hanover, J. A. Mutational analysis of the catalytic domain of O- linked N-acetylglucosaminyl transferase. J Biol Chem 280, 35537-44 (2005).

8. Martinez-Fleites, C. et al. Structure of an O-GlcNAc transferase homolog provides insight into intracellular glycosylation. Nat Struct Mol Biol 15, 764-5 (2008).

9. Copeland, R.J., Bullen, J.W. & Hart, G.W. Cross-talk between GlcNAcylation and

phosphorylation: roles in insulin resistance and glucose toxicity. Am J Physiol Endocrinol Metab 295, E17-28 (2008).

10. Housley, M.P. et al. O-GlcNAc regulates FoxO activation in response to glucose. J Biol Chem 283, 16283-92 (2008).

11. Klein, A.L., Berkaw, M.N., Buse, M.G. & Ball, L.E. O-linked N-acetylglucosamine modification of 14 insulin receptor substrate- 1 occurs in close proximity to multiple SH2 domain binding motifs. Mol Cell Proteomics 8, 2733-45 (2009).

12. Wang, Z. et al. Enrichment and site mapping of O-linked N-acetylglucosamine by a combination of chemical/enzymatic tagging, photochemical cleavage, and electron transfer dissociation mass spectrometry. Mol Cell Proteomics 9, 153-60 (2010).

13. Hart, G.W. & Akimoto, Y. The O-GlcNAc modification. Essentials ofglycobiology, chapter 18.

14. Khidekel, N. et al. Probing the dynamics of O-GlcNAc glycosylation in the brain using quantitative proteomics. Nat Chem Biol 3, 339-48 (2007).

15. Wells, L. et al. Mapping sites of O-GlcNAc modification using affinity tags for serine and threonine post-translational modifications. Mol Cell Proteomics 1, 791-804 (2002).

16. Lubas, W.A., Smith, M., Starr, CM. & Hanover, J. A. Analysis of nuclear pore protein p62 glycosylation. Biochemistry 34, 1686-94 (1995).

17. Housley, M.P. et al. A PGC-lalpha-O-GlcNAc transferase complex regulates FoxO transcription factor activity in response to glucose. J Biol Chem 284, 5148-57 (2009).

18. Wang, Z. et al. Extensive crosstalk between O-GlcNAcylation and phosphorylation regulates cytokinesis. Sci Signal 3, ra2 (2010).

19. Boggon, T.J. & Shapiro, L. Screening for phasing atoms in protein crystallography. Structure 8, R143-9 (2000).

20. Leslie, A.G.W. Recent changes to the MOSFLM package for processing film and image plate data. Joint CCP4 + ESF-EAMCB Newsletter on Protein Crystallography 26(1992). 21. Evans, P. Scaling and assessment of data quality. Acta Crystallogr D Biol Crystallogr 62, 72- 82 (2006).

22. de la Fortelle, E. & Bricogne, G. Maximum-Likelihood Heavy- Atom Parameter Refinement for the Multiple Isomorphous Replacement and Multiwavelength Anomalous Diffraction Methods. Methods Enzymol 276, 472-494 (1997).

23. Pape, T. & Schneider, T.R. HKL2MAP: a graphical user interface for phasing with SHELX programs. J. Appl. Cryst. 37, 843-844 (2004).

24. McCoy, A.J. et al. Phaser crystallographic software. J Appl Crystallogr 40, 658-674 (2007).

25. The CCP4 suite: programs for protein crystallography. Acta Crystallogr D Biol Crystallogr 50, 760-3 (1994).

26. Brunger, A.T. et al. Crystallography & NMR system: A new software suite for

macromolecular structure determination. Acta Crystallogr D Biol Crystallogr 54, 905-21 (1998).

27. Emsley, P. & Cowtan, K. Coot: model-building tools for molecular graphics. Acta

Crystallogr D Biol Crystallogr 60, 2126-32 (2004).

28. Adams, P.D. et al. ΡΗΕΝΓΧ: a comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr D Biol Crystallogr 66, 213-21.

29. Painter, J. & Merritt, E.A. TLSMD web server for the generation of multi-group TLS models. /. Appl. Cryst. 39, 109-111 (2006).

30. Painter, J. & Merritt, E.A. Optimal description of a protein structure in terms of multiple groups undergoing TLS motion. Acta Crystallogr D Biol Crystallogr 62, 439-50 (2006).

31. DeLano, W.L. The Pymol Molecular Graphics System. (Delano Scientific, San Carlos, CA, USA, 2002).

32. Potterton, L. et al. Developments in the CCP4 molecular-graphics project. Acta Crystallogr D Biol Crystallogr 60, 2288-94 (2004).

33. McCoy, A.J. Solving structures of protein complexes by molecular replacement with Phaser. Acta Crystallogr D Biol Crystallogr 63, 32-41 (2007).

Example 2

[00207] A crystal structure (1.7 A) was obtained from a crystallizable composition comprising I1OGT4.5, UDP-GlcNAc, and peptide substrate using the methods described in Example 1 and Methods above for the OGT-UDP-peptide complex. OGT-UDP-peptide complex crystals were used to seed crystallization. The glycosylation reaction took place in the crystal; thus the crystal obtained was a ternary complex of OGT, UDP, and glycopeptide. The coordinates of the OGT-UDP-glycopeptide complex are found in Table 7. Certain sugar-protein contacts were gleaned from the OGT-UDP-glycopeptide complex; namely, His 498 contacts the C2 acetamide oxygen of the sugar, His 920 contacts the C3 hydroxyl of the sugar, Leu 653 backbone carbonyl contacts the C4 hydroxyl of the sugar, and Thr 560 contacts the C6 hydroxyl of the sugar.

EQUIVALENTS AND SCOPE

[00208] Those skilled in the art will recognize or be able to ascertain using no more than routine experimentation many equivalents to the specific embodiments described herein. The scope of the present invention is not intended to be limited to the above Description, but rather is as set forth in the appended claims.

[00209] In the claims articles such as "a," "an," and "the" may mean one or more than one unless indicated to the contrary or otherwise evident from the context. Claims or descriptions that include "or" between one or more members of a group are considered satisfied if one, more than one, or all of the group members are present in, employed in, or otherwise relevant to a given product or process unless indicated to the contrary or otherwise evident from the context. The invention includes embodiments in which exactly one member of the group is present in, employed in, or otherwise relevant to a given product or process. The invention includes embodiments in which more than one, or all of the group members are present in, employed in, or otherwise relevant to a given product or process. Furthermore, it is to be understood that the invention encompasses all variations, combinations, and permutations in which one or more limitations, elements, clauses, descriptive terms, etc., from one or more of the listed claims is introduced into another claim. For example, any claim that is dependent on another claim can be modified to include one or more limitations found in any other claim that is dependent on the same base claim. Furthermore, where the claims recite a composition, it is to be understood that methods of using the composition for any of the purposes disclosed herein are included, and methods of making the composition according to any of the methods of making disclosed herein or other methods known in the art are included, unless otherwise indicated or unless it would be evident to one of ordinary skill in the art that a contradiction or inconsistency would arise. [00210] Where elements are presented as lists, e.g., in Markush group format, it is to be understood that each subgroup of the elements is also disclosed, and any element(s) can be removed from the group. It should it be understood that, in general, where the invention, or aspects of the invention, is/are referred to as comprising particular elements, features, etc. , certain embodiments of the invention or aspects of the invention consist, or consist essentially of, such elements, features, etc. For purposes of simplicity those embodiments have not been specifically set forth in haec verba herein. It is also noted that the term "comprising" is intended to be open and permits the inclusion of additional elements or steps.

[00211] Where ranges are given, endpoints are included. Furthermore, it is to be understood that unless otherwise indicated or otherwise evident from the context and

understanding of one of ordinary skill in the art, values that are expressed as ranges can assume any specific value or subrange within the stated ranges in different embodiments of the invention, to the tenth of the unit of the lower limit of the range, unless the context clearly dictates otherwise.

[00212] In addition, it is to be understood that any particular embodiment of the present invention that falls within the prior art may be explicitly excluded from any one or more of the claims. Since such embodiments are deemed to be known to one of ordinary skill in the art, they may be excluded even if the exclusion is not set forth explicitly herein. Any particular embodiment of the compositions of the invention can be excluded from any one or more claims, for any reason, whether or not related to the existence of prior art.

APPENDIX

Sequences:

human wild- type O-GlcNAc transferase (SEQ ID NO.: 53)

MASSVGNVADSTGLAELAHREYQAGDFEAAERHCMQLWRQEPDNTGVLLLLSS IHFQCRRLDRS AHFSTLAIKQNPLLAEAYSNLGNVYKERGQLQEAIEHYRHALRLKPDFIDGYINLAAALVAAGD MEGAVQAYVSALQYNPDLYCVRSDLGNLLKALGRLEEAKACYLKAIETQPNFAVAWSNLGCVFN AQGEIWLAIHHFEKAVTLDPNFLDAYINLGNVLKEARIFDRAVAAYLRALSLSPNHAVVHGNLA CVYYEQGLIDLAIDTYRRAIELQPHFPDAYCNLANALKEKGSVAEAEDCYNTALRLCPTHADSL NNLA IKREQG IEEAVRLYRKALEVFPEFAAAHSNLASVLQQQGKLQEALMHYKEAIRI SPTF ADAYSNMGNTLKEMQDVQGALQCYTRAIQINPAFADAHSNLAS IHKDSG IPEAIASYRTALKL KPDFPDAYCNLAHCLQIVCDWTDYDERMKKLVS IVADQLEKNRLPSVHPHHSMLYPLSHGFRKA IAERHGNLCLDKINVLHKPPYEHPKDLKLSDGRLRVGYVSSDFGNHPTSHLMQS IPGMHNPDKF EVFCYALSPDDGTNFRVKVMAEANHFIDLSQIPCNGKAADRIHQDGIHILVNMNGYTKGARNEL FALRPAPIQAMWLGYPGTSGALFMDYI ITDQETSPAEVAEQYSEKLAYMPHTFFIGDHANMFPH LKKKAVIDFKSNGHIYDNRIVLNGIDLKAFLDSLPDVKIVKMKCPDGGDNADSSNTALNMPVIP MNTIAEAVIEMINRGQIQITINGFS I SNGLATTQINNKAATGEEVPRTI IVTTRSQYGLPEDAI VYCNFNQLYKIDPSTLQMWA ILKRVPNSVLWLLRFPAVGEP IQQYAQNMGLPQNRI IFSPVA PKEEHVRRGQLADVCLDTPLCNGHTTGMDVLWAGTPMVTMPGETLASRVAASQLTCLGCLELIA KNRQEYEDIAVKLGTDLEYLKKVRGKVWKQRI SSPLFNTKQYTMELERLYLQMWEHYAAGNKPD HMIKPVEVTESA (SEQ ID NO: 53) hOGT4.5 (amino acids 313-1028, SEQ ID NO: 54)

GPGSCPTHADSLNNLANIKREQGNIEEAVRLYRKALEVFPEFAAAHSNLASVLQQQGKLQEALM HYKEAIRI SPTFADAYSNMGNTLKEMQDVQGALQCYTRAIQINPAFADAHSNLAS IHKDSG IP EAIASYRTALKLKPDFPDAYCNLAHCLQIVCDWTDYDERMKKLVS IVADQLEKNRLPSVHPHHS MLYPLSHGFRKAIAERHGNLCLDKINVLHKPPYEHPKDLKLSDGRLRVGYVSSDFGNHPTSHLM QSIPGMHNPDKFEVFCYALSPDDGTNFRVKVMAEANHFIDLSQIPCNGKAADRIHQDGIHILVN MNGYTKGARNELFALRPAPIQAMWLGYPGTSGALFMDYI ITDQETSPAEVAEQYSEKLAYMPHT FFIGDHANMFPHLKKKAVIDFKSNGHIYDNRIVLNGIDLKAFLDSLPDVKIVKMKCPDGGDNAD SSNTALNMPVIPMNTIAEAVIEMINRGQIQITINGFS I SNGLATTQINNKAATGEEVPRTI IVT TRSQYGLPEDAIVYCNFNQLYKIDPSTLQMWANILKRVPNSVLWLLRFPAVGEPNIQQYAQNMG LPQNRI IFSPVAPKEEHVRRGQLADVCLDTPLCNGHTTGMDVLWAGTPMVTMPGETLASRVAAS QLTCLGCLELIAKNRQEYEDIAVKLGTDLEYLKKVRGKVWKQRI SSPLFNTKQYTMELERLYLQ MWEHYAAGNKPDHMIKPVE (SEQ ID NO: 54) UDP Complex UDP-CKII Peptide

Complex

Data Collection Statistics

Beam Line NSLS x29 NSLS x25

Space Group P321 1121

Wavelength (A) 1.0809 1.0000

Number of Reflections 154231 141571

Cell dimensions

a, b, c (A) 273.6592, 273.6592, 143.0501 98.538, 136.66, 153.54 , β, γ (°) 90.0, 90.0, 120.0 90.0, 102.90, 90.0

Resolution (A)a 50-2.775 (2.93 - 2.775) 30-1.95 (2.06-1.95)

Rsym or Rmerge 0.116 (0.425) 0.098 (0.180)

I/sI 8.4 (3.0) 8.4 (4.7)

Completeness 98.2 (95.1) 98.4 (94.5)

Redundancy 3.3 (3.1) 3.1 (2.8)

Refinement Statistics

Resolution (A) 48.59 - 2.775 30-1.95

No. Reflections 151011 141555

Reflections (work/test) 148987 / 2024 134456 / 7099

Rwork / Rfree % 17.4 / 22.3 22.4 / 25.2

Number of OGT molecules/asymmetric unit 4 2

Number of modeled OGT residues/chain 701 on all four monomers 695 for chain A / 674 chain C

Number of water molecules 286 860

Number of S04 ions 3

Average B-Factors

OGT 48.733 21.710

UDP 35.999 9.373

Peptide 20.149

Solvent 36.872 24.474

R.m.s. deviations

Bond Lengths (A) 0.008 0.007

Bond Angles (°) 1.106 1.052

Ramachandran (number of residues / %)

Most favored 2223 / 90.1% 1116 / 91.5%

Additionally Allowed 240 / 9.7% 102 / 8.4%

Generally Allowed 1 / 0.0% 0 / 0%

Disallowed 4 / 0.2% 2 / 0.2%

Residues in disallowed region Thr 669, Leu 653 Leu 653

aValues in parentheses are from highest resolution shell.

Table 1 X-ray data collection and model refinement statistics of OGT-UDP and OGT-UDP-peptide complexes.

Potassium platinum Sodium aurothiomalate Potassium platinum Potassium platinum tetrachloride derivative derivative tetrabromide derivative tetrachloride derivative

Data Collection

Statistics

Beam Line BNL x29 APS ID24C BNL x29 BNL x29

Space Group P321 P321 P321 P321

Wavelength (A) 1.0715 1.0384 1.0715 1.0715

Number of Reflections 38280 (5632) 30134 (4412) 12120 (1768) 92019 (13411)

Cell dimensions

a, b, c (A) 273.2, 273.2, 142.8 274.3, 274.3, 143.0 271.9, 271.9, 141.9 274.1, 274.1, 142.7 α, β} γ (°) 90.0, 90.0, 120.0 90.0, 90.0, 120.0 90.0, 90.0, 120.0 90.0, 90.0, 120.0

Resolution (A)J 44.92-4.40 (4.64-4.40) 42.10-4.8 (5.06-4.80) 48.32-6.5 (6.85-6.5) 48.69-3.30(3.48-3.30)

Rsym or Rmerge 0.107 (0.409) 0.095 (0.382) 0.072 (0.358) 0.099 (0.346)

Ι/σΙ 8.4 (3.5) 9.9 (4.2) 15.6 (4.3) 9.7 (4.0)

Completeness 98.1 (99.5) 98.8 (99.6) 99.5 (100.0) 99.5 (99.9)

Redundancy 3.8 (3.8) 4.1 (4.2) 5.2 (5.3) 3.9 (3.9)

Values in parentheses are from highest resolution shell.

Table 2. X-ray data collection statistics of heavy atom derivatives.

Mutant <10% 10-30% 30-50% 75-100% Reference

Activity Activity Activity Activity

D431A (4) N458A (4) H498A this study and (4)

H499A this study D523A (7) H558A this study and (8)

R637A (4) Q839N (8) Y841A (8) K842A (8) K842M (8) K898A (4) and (8) H901A this study H920A (8) T921A (8) D925A (4) K981A/K982A this study and (10) AInta this study

K706S/K707S/K742S/K745S/K747S this study K714S/K742S/K745S/K747S this study K706S/K707S this study K714S this study K742S/K457S/K747S this study

Table 3. Summary of the enzymatic activity of OGT mutants reported in the literature and made in this study.

Mutants made by us were tested as described in the Examples.

Table 4. O-GlcNAcylation sites on OGT protein substrates reported in the literature. Only sequences containing known GlcNAcylation sites have been listed. The glycosylation sites are shown in underline.

Table 5. Atomic coordinates of a crystalline OGT binary complex can be found in the Protein Data Bank, PDB Code 3PE3.

REMARK Date 2010-04-13 Time 21:29:52 EDT -0400 (1271208592.53 s)

REMARK PHENIX refinement

REMARK

REMARK ****************** INPUT FILES AND LABELS REMARK Reflections:

REMARK file name : mbl205_final_scala_800_mos08Rfree.mtz

REMARK labels : ['F_mbl205,SIGF_mbl205']

REMARK R-free flags:

REMARK file name : mbl205_final_scala_800_mos08Rfree.mtz

REMARK label : FreeR_flag

REMARK test_flag_value: 0

REMARK Model file name(s):

REMARK

/nfs/xray/walkerlab/lazarus/ogt/mbl205_final/final_minimized_mbl205_petide_2.pdb REMARK

REMARK ******************** REFINEMENT SUMMARY: QUICK FACTS

REMARK Start: r_work = 0.2258 r_free = 0.2537 bonds = 0.008 angles = 1.058 REMARK Final: r_work = 0.2241 r_free = 0.2521 bonds = 0.007 angles = 1.052 REMARK

REMARK

REMARK ****************** REFINEMENT STATISTICS STEP BY STEP

REMARK leading digit, like 1_, means number of macro-cycle

REMARK 0 : statistics at the very beginning when nothing is done yet

REMARK l_bss: bulk solvent correction and/or (anisotropic) scaling

REMARK l_xyz: refinement of coordinates

REMARK l_adp: refinement of ADPs (Atomic Displacement Parameters)

REMARK

REMARK R-factors, x-ray target values and norm of gradient of x-ray target REMARK stage r- work r-free xray_target_w xray_target_t

REMARK 0 : 0.2717 0.2949 6.558639e+00 6.663175e+00

REMARK l_bss: 0.2258 0.2537 6.480023e+00 6.59443 le+00

REMARK l_xyz: 0.2257 0.2537 6.479928e+00 6.594923e+00

REMARK l_adp: 0.2255 0.2536 6.477422e+00 6.594122e+00

REMARK 2_bss: 0.2255 0.2536 6.477422e+00 6.594119e+00

REMARK 2_xyz: 0.2255 0.2536 6.477375e+00 6.594052e+00

REMARK 2_adp: 0.2252 0.2532 6.475319e+00 6.591597e+00

REMARK 3_bss: 0.2252 0.2530 6.475115e+00 6.591474e+00

REMARK 3_xyz: 0.2251 0.2530 6.474714e+00 6.591133e+00

REMARK 3_adp: 0.2241 0.2521 6.470541e+00 6.587895e+00

REMARK 3_bss: 0.2241 0.2521 6.470541e+00 6.587895e+00

REMARK

REMARK stage k_sol b_sol bl l b22 b33 bl2 bl3 b23 REMARK 0 : 0.000 0.000 0.000 0.000 0.000 0.000 0.000 0 000 REMARK l_bss: 0.410 40.755 -2.746 -1.495 4.241 -0.000 3.148 -0.000 REMARK l_xyz: 0.410 40.755 -2.746 -1.495 4.241 -0.000 3.148 -0.000 REMARK l_adp: 0.410 40.755 -2.746 -1.495 4.241 -0.000 3.148 -0.000 REMARK 2_bss: 0.410 40.748 -2.746 -1.495 4.241 -0.000 3.148 -0.000 REMARK 2_xyz: 0.410 40.748 -2.746 -1.495 4.241 -0.000 3.148 -0.000 REMARK 2_adp: 0.410 40.748 -2.746 -1.495 4.241 -0.000 3.148 -0.000 REMARK 3_bss: 0.410 40.765 -2.563 -1.508 4.072 -0.000 3.120 -0.000 REMARK 3_xyz: 0.410 40.765 -2.563 -1.508 4.072 -0.000 3.120 -0.000 REMARK 3_adp: 0.410 40.765 -2.563 -1.508 4.072 -0.000 3.120 -0.000 REMARK 3 bss: 0.410 40.765 -2.563 -1.508 4.072 -0.000 3.120 0.000 REMARK REMARK stage <pher> fom alpha beta

REMARK 0 : 27.444 0.7987 0.8751 144575.003

REMARK 1 bss: 24.862 0.8270 0.9096 108733.736

REMARK l_xyz: 24.877 0.8269 0.9094 108719.169

REMARK l_adp: 24.832 0.8273 0.8965 108424.791

REMARK 2_bss: 24.832 0.8273 0.8965 108422.736

REMARK 2_xyz: 24.830 0.8274 0.8964 108453.302

REMARK 2_adp: 24.738 0.8283 0.8938 108001.337

REMARK 3_bss: 24.722 0.8285 0.8948 107950.093

REMARK 3_xyz: 24.708 0.8286 0.8949 107928.395

REMARK 3_adp: 24.602 0.8297 0.8975 107144.370

REMARK 3_bss: 24.602 0.8297 0.8975 107144.370

REMARK REMARK stage angl bond chir dihe plan repu geom_target

REMARK 0 : 1.058 0.008 0.071 16.383 0.005 4.111 6.9384e-02 REMARK l_bss: 1.058 0.008 0.071 16.383 0.005 4.111 6.9384e-02 REMARK l_xyz: 1.054 0.007 0.071 16.365 0.005 4.111 6.8767e-02 REMARK l_adp: 1.054 0.007 0.071 16.365 0.005 4.111 6.8767e-02 REMARK 2_bss: 1.054 0.007 0.071 16.365 0.005 4.111 6.8767e-02 REMARK 2_xyz: 1.049 0.007 0.070 16.353 0.005 4.111 6.8239e-02 REMARK 2_adp: 1.049 0.007 0.070 16.353 0.005 4.111 6.8239e-02 REMARK 3_bss: 1.049 0.007 0.070 16.353 0.005 4.111 6.8239e-02 REMARK 3_xyz: 1.052 0.007 0.071 16.353 0.005 4.111 6.8453e-02 REMARK 3_adp: 1.052 0.007 0.071 16.353 0.005 4.111 6.8453e-02 REMARK 3_bss: 1.052 0.007 0.071 16.353 0.005 4.111 6.8453e-02 REMARK REMARK Maximal deviations:

REMARK stage angl bond chir dihe plan repu Igradl

REMARK 0 : 11.462 0.069 0.288131.900 0.061 2.302 2.7685e-02 REMARK l_bss: 11.462 0.069 0.288131.900 0.061 2.302 2.7685e-02 REMARK l_xyz: 11.614 0.068 0.287131.697 0.045 2.299 2.6426e-02 REMARK l_adp: 11.614 0.068 0.287131.697 0.045 2.299 2.6426e-02 REMARK 2_bss: 11.614 0.068 0.287131.697 0.045 2.299 2.6426e-02 REMARK 2_xyz: 11.469 0.067 0.284131.868 0.044 2.314 2.5881e-02 REMARK 2_adp: 11.469 0.067 0.284131.868 0.044 2.314 2.588 le-02 REMARK 3_bss: 11.469 0.067 0.284131.868 0.044 2.314 2.5881e-02

REMARK 3_xyz: 11.521 0.070 0.282132.318 0.045 2.312 2.6074e-02

REMARK 3_adp: 11.521 0.070 0.282132.318 0.045 2.312 2.6074e-02

REMARK 3_bss: 11.521 0.070 0.282132.318 0.045 2.312 2.6074e-02

REMARK REMARK I overall 1— -macromolecule— I solvent 1

REMARK stage b_max b_min b_ave b_max b_min b_ave b_max b_min b. ave REMARK 0 : 107.83 2.29 21.63 107.83 2.29 21.43 59.97 4.98 24.28 REMARK l_bss: 107.78 2.28 22.01 107.78 2.28 21.85 59.85 4.86 24.16 REMARK l_xyz: 107.78 2.28 22.01 107.78 2.28 21.85 59.85 4.86 24.16 REMARK l_adp: 107.05 2.19 21.61 107.05 2.19 21.41 60.01 4.63 24.15 REMARK 2_bss: 107.05 2.19 21.61 107.05 2.19 21.41 60.01 4.63 24.15 REMARK 2_xyz: 107.05 2.19 21.61 107.05 2.19 21.41 60.01 4.63 24.15 REMARK 2_adp: 105.13 2.19 21.54 105.13 2.19 21.34 60.03 4.54 24.11 REMARK 3_bss: 105.15 2.21 21.56 105.15 2.21 21.36 60.05 4.56 24.13 REMARK 3_xyz: 105.15 2.21 21.56 105.15 2.21 21.36 60.05 4.56 24.13 REMARK 3_adp: 105.17 2.38 21.84 105.17 2.38 21.65 60.18 4.77 24.20 REMARK 3 bss: 105.17 2.38 21.84 105.17 2.38 21.65 60.18 4.77 24.20 REMARK REMARK stage Deviation of refined

REMARK model from start model

REMARK max min mean

REMARK 0 : 0.000 0.000 0.000

REMARK l_bss: 0.000 0.000 0.000

REMARK l_xyz 0.481 0.000 0.008

REMARK l_adp 0.481 0.000 0.008

REMARK 2_bss: 0.481 0.000 0.008

REMARK 2_xyz 0.503 0.000 0.007

REMARK 2_adp 0.503 0.000 0.007

REMARK 3_bss: 0.503 0.000 0.007

REMARK 3_xyz 0.526 0.000 0.009

REMARK 3_adp 0.526 0.000 0.009

REMARK 3 bss: 0.526 0.000 0.009

REMARK REMARK MODEL CONTENT.

REMARK ELEMENT ATOM RECORD COUNT OCCUPANCY SUM REMARK P 4 4.00

REMARK C 7088 7013.00

REMARK S 81 81.00

REMARK o 2936 2918.00

REMARK N 1933 1924.00

REMARK TOTAL 12042 11940.00

REMARK REMARK r_free_flags.md5.hexdigest fb270c91dfealc357055ce20c439df61

REMARK REMARK IF THIS FILE IS FOR PDB DEPOSITION: REMOVE ALL FROM THIS LINE UP. REMARK 3

REMARK 3 REFINEMENT.

REMARK 3 PROGRAM : PHENIX (phenix .refine: 1.6_289)

REMARK 3 AUTHORS : Adams,Afonine,Chen,Davis,Echols,Gopal,

REMARK 3 : Grosse-Kunstleve,Headd,Hung,Immormino,Ioerger,McCoy,

REMARK 3 : McKee,Moriarty,Pai,Read,Richardson,Richardson,Romo,

REMARK 3 : Sacchettini,Sauter,Smith,Storoni,Terwilliger,Zwart

REMARK 3

REMARK 3 REFINEMENT TARGET : ML

REMARK 3

REMARK 3 DATA USED IN REFINEMENT.

REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.950

REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.981

REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.34

REMARK 3 COMPLETENESS FOR RANGE (%) : 98.38

REMARK 3 NUMBER OF REFLECTIONS : 141555

REMARK 3

REMARK 3 FIT TO DATA USED IN REFINEMENT.

REMARK 3 R VALUE (WORKING + TEST SET) : 0.2255

REMARK 3 R VALUE (WORKING SET) : 0.2241

REMARK 3 FREE R VALUE : 0.2521

REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.02

REMARK 3 FREE R VALUE TEST SET COUNT : 7099

REMARK 3

REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).

REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE

REMARK 3 1 29.9848 - 6.0431 0.98 4539 243 0.2941 0.2819

REMARK 3 2 6.0431 - 4.8030 0.94 4291 226 0.2416 0.2655

REMARK 3 3 4.8030 - 4.1977 0.97 4480 245 0.2093 0.2291

REMARK 3 4 4.1977 - 3.8147 0.99 4534 228 0.2034 0.2281

REMARK 3 5 3.8147 - 3.5418 0.99 4514 254 0.2087 0.2067

REMARK 3 6 3.5418 - 3.3333 0.99 4540 248 0.2184 0.2550

REMARK 3 7 3.3333 - 3.1665 0.99 4524 248 0.2268 0.2501

REMARK 3 8 3.1665 - 3.0288 0.99 4509 236 0.2261 0.2391

REMARK 3 9 3.0288 - 2.9123 1.00 4543 259 0.2320 0.2579

REMARK 3 10 2.9123 - 2.8119 0.99 4503 243 0.2306 0.2484

REMARK 3 11 2.8119 - 2.7240 0.99 4551 219 0.2271 0.2605

REMARK 3 12 2.7240 - 2.6462 0.99 4572 205 0.2215 0.2600

REMARK 3 13 2.6462 - 2.5766 1.00 4541 220 0.2152 0.2495

REMARK 3 14 2.5766 - 2.5138 0.99 4527 248 0.2182 0.2519

REMARK 3 15 2.5138 - 2.4566 0.99 4518 236 0.2133 0.2505

REMARK 3 16 2.4566 - 2.4044 0.99 4494 271 0.2100 0.2505

REMARK 3 17 2.4044 - 2.3563 1.00 4493 255 0.2181 0.2805

REMARK 3 18 2.3563 - 2.3119 0.99 4553 220 0.2155 0.2474

REMARK 3 19 2.3119 - 2.2706 0.99 4531 238 0.2133 0.2535 REMARK 3 20 2.2706 - 2.2321 0.99 4502 258 0.2129 0.2782

REMARK 3 21 2.2321 - 2.1961 0.99 4501 243 0.2092 0.2497

REMARK 3 22 2.1961 - 2.1623 1.00 4500 242 0.2019 0.2559

REMARK 3 23 2.1623 - 2.1305 0.99 4515 232 0.2005 0.2236

REMARK 3 24 2.1305 - 2.1005 0.99 4555 244 0.2023 0.2517

REMARK 3 25 2.1005 - 2.0722 0.99 4559 210 0.2000 0.2516

REMARK 3 26 2.0722 - 2.0453 1.00 4484 217 0.1901 0.2293

REMARK 3 27 2.0453 - 2.0197 0.99 4510 239 0.1923 0.2587

REMARK 3 28 2.0197 - 1.9954 0.96 4369 244 0.1950 0.2339

REMARK 3 29 1.9954 - 1.9722 0.93 4211 224 0.2078 0.2472

REMARK 3 30 1.9722 - 1.9500 0.87 3993 204 0.2186 0.2750

REMARK 3

REMARK 3 BULK SOLVENT MODELLING.

REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL

REMARK 3 SOLVENT RADIUS 1.11

REMARK 3 SHRINKAGE RADIUS : 0.90

REMARK 3 GRID STEP FACTOR 4.00

REMARK 3 K_SOL : 0.410

REMARK 3 B SOL : 40.765

REMARK 3

REMARK 3 ERROR ESTIMATES.

REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.27 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.60 REMARK 3

REMARK 3 OVERALL SCALE FACTORS.

REMARK 3 SCALE = SUM(IF_OBSI*IF_MODELI)/SUM(IF_MODELI**2) : 0.9662 REMARK 3 ANISOTROPIC SCALE MATRIX ELEMENTS (IN CARTESIAN BASIS). REMARK 3 Bl l -2.5632

REMARK 3 B22 -1.5083

REMARK 3 B33 4.0715

REMARK 3 B12 -0.0000

REMARK 3 B13 3.1197

REMARK 3 B23 -0.0000

REMARK 3

REMARK 3 R FACTOR FORMULA.

REMARK 3 R = SUM(IIF_OBSI-SCALE*IF_MODELII)/SUM(IF_OBSI)

REMARK 3

REMARK 3 TOTAL MODEL STRUCTURE FACTOR (F_MODEL).

REMARK 3 F_MODEL = FB_CART * (F_CALC_ATOMS + F_BULK)

REMARK F_BULK = K_SOL * EXP(-B_SOL * S**2 / 4) * F_MASK

REMARK F_CALC_ATOMS = ATOMIC MODEL STRUCTURE FACTORS REMARK FB_CART = EXP(-H(t) * A(-l) * B * A(-lt) * H)

REMARK A = orthogonalization matrix, H = MILLER INDEX

REMARK (t) = TRANSPOSE, (-1) = INVERSE

REMARK REMARK STRUCTURE FACTORS CALCULATION ALGORITHM : FFT REMARK 3

REMARK 3 DEVIATIONS FROM IDEAL VALUES.

REMARK 3 RMSD MAX COUNT

REMARK 3 BOND : 0.007 0.070 11453

REMARK 3 ANGLE : 1.052 11.521 15573

REMARK 3 CHIRALITY : 0.071 0.282 1722

REMARK 3 PLANARITY : 0.005 0.045 2020

REMARK 3 DIHEDRAL : 16.353 132.318 4245

REMARK 3 MIN NONBONDED DISTANCE : 2.312

REMARK 3

REMARK 3 ATOMIC DISPLACEMENT PARAMETERS.

REMARK 3 WILSON B : 17.47

REMARK 3 RMS(B_ISO_OR_EQUIVALENT_BONDED) : 6.04

REMARK 3 ATOMS NUMBER OF ATOMS

REMARK 3 ISO. ANISO.

REMARK 3 ALL : 12042 11117

REMARK 3 ALL (NO H) : 12042 11117

REMARK 3 SOLVENT : 860 0

REMARK 3 NON-SOLVENT : 11182 11117

REMARK 3 HYDROGENS : 0 0

REMARK 3

REMARK 3 TLS DETAILS.

REMARK 3 NUMBER OF TLS GROUPS: 21

REMARK 3 ORIGIN: CENTER OF MASS

REMARK 3 TLS GROUP : 1

REMARK 3 SELECTION: (chain A and resid 315:334)

REMARK 3 ORIGIN FOR THE GROUP (A): -13.8974 36.3941 -36.2867

REMARK 3 T TENSOR

REMARK 3 Ti l: 0.2933 T22: 0.3718

REMARK 3 T33: 0.2987 T12: 0.0150

REMARK 3 T13: -0.0455 T23: 0.1597

REMARK 3 L TENSOR

REMARK 3 Ll l 0.1358 L22 0.4420

REMARK 3 L33 0.3083 L12 -0.2389

REMARK 3 L13 0.1904 L23 -0.3492

REMARK 3 S TENSOR

REMARK 3 Sl l: -0.1484 S12: -0.1690 S13: 0.0097

REMARK 3 S21: -0.2575 S22: 0.1242 S23: 0.3016

REMARK 3 S31: -0.0760 S32: -0.2687 S33: -0.1575

REMARK 3 TLS GROUP : 2

REMARK 3 SELECTION: (chain A and resid 335:348)

REMARK 3 ORIGIN FOR THE GROUP (A): -6.3958 32.4680 -37.3108

REMARK 3 T TENSOR

REMARK 3 Ti l 0.3106 T22: 0.2844

REMARK 3 T33 0.1783 T12: -0.0073

REMARK 3 T13 -0.0920 T23: 0.0854 REMARK 3 L TENSOR

REMARK 3 Ll l 0.4062 L22: 0.5153

REMARK 3 L33 0.9044 L12: 0.4228

REMARK 3 L13 -0.6029 L23: -0.6368

REMARK 3 S TENSOR

REMARK 3 Sl l 0.1375 S12: -0.1068 S13: -0.0538

REMARK 3 S21 -0.3244 S22: 0.1521 S23: 0.0840

REMARK 3 S31 0.1834 S32: 0.2112 S33: 0.0736

REMARK 3 TLS GROUP : 3

REMARK 3 SELECTION: (chain A and resid 349:456)

REMARK 3 ORIGIN FOR THE GROUP (A): -5.1353 41.0677 14.9634

REMARK 3 T TENSOR

REMARK 3 Ti l 0.0811 T22: 0.0868

REMARK 3 T33 0.0284 T12: 0.0329

REMARK 3 T13 0.0278 T23: 0.0407

REMARK 3 L TENSOR

REMARK 3 Ll l 0.6899 L22: 0.3884

REMARK 3 L33 0.0074 L12: -0.0553

REMARK 3 L13 -0.0692 L23: 0.0440

REMARK 3 S TENSOR

REMARK 3 Sl l 0.0509 S12: 0.2237 S13: 0.0294

REMARK 3 S21 0.0132 S22: 0.0763 S23: 0.0063

REMARK 3 S31 -0.0146 S32: -0.0645 S33: -0.0679

REMARK 3 TLS GROUP : 4

REMARK 3 SELECTION: (chain A and resid 457:514)

REMARK 3 ORIGIN FOR THE GROUP (A): -25.2079 44.3532 -2.8039

REMARK 3 T TENSOR

REMARK 3 Ti l 0.1282 T22: 0.0633

REMARK 3 T33 0.0482 T12: 0.0671

REMARK 3 T13 0.0290 T23: 0.0395

REMARK 3 L TENSOR

REMARK 3 Ll l 0.2038 L22: 0.3641

REMARK 3 L33 0.2849 L12: -0.0336

REMARK 3 L13 0.1915 L23: -0.2320

REMARK 3 S TENSOR

REMARK 3 Sl l 0.1181 S12: 0.0892 S13: 0.0463

REMARK 3 S21 -0.0636 S22: 0.0004 S23: 0.0301

REMARK 3 S31 0.0537 S32: -0.0300 S33: -0.0440

REMARK 3 TLS GROUP : 5

REMARK 3 SELECTION: (chain A and resid 515:712)

REMARK 3 ORIGIN FOR THE GROUP (A): -25.5110 16.7231 -2.2769

REMARK 3 T TENSOR

REMARK 3 Ti l 0.1678 T22: 0.0767

REMARK 3 T33 0.0083 T12: 0.0411

REMARK 3 T13 -0.0365 T23: -0.0057

REMARK 3 L TENSOR REMARK 3 Ll l 0.0835 L22: 0.5996

REMARK 3 L33 0.2698 L12: -0.1138

REMARK 3 L13 -0.0694 L23: -0.0381

REMARK 3 S TENSOR

REMARK 3 Sl l 0.0765 S12: 0.0882 S13: -0.0113

REMARK 3 S21 -0.2465 S22: -0.0521 S23: 0.0683

REMARK 3 S31 0.0991 S32: 0.0001 S33: -0.0121

REMARK 3 TLS GROUP : 6

REMARK 3 SELECTION: (chain A and resid 713:718)

REMARK 3 ORIGIN FOR THE GROUP (A): -15.8223

REMARK 3 T TENSOR

REMARK 3 Ti l 0.6782 T22: 0.3020

REMARK 3 T33 0.3290 T12: 0.1151

REMARK 3 T13 -0.2754 T23: 0.0680

REMARK 3 L TENSOR

REMARK 3 Ll l 0.1076 L22: 0.5717

REMARK 3 L33 0.7188 L12: 0.0451

REMARK 3 L13 -0.1647 L23: -0.5620

REMARK 3 S TENSOR

REMARK 3 Sl l 0.0092 S12: -0.0027 S13: -0.0167

REMARK 3 S21 0.3560 S22: -0.0642 S23: -0.0324

REMARK 3 S31 -0.1723 S32: 0.0971 S33: 0.0335

REMARK 3 TLS GROUP : 7

REMARK 3 SELECTION: (chain A and resid 719:744)

REMARK 3 ORIGIN FOR THE GROUP (A): -17.2475 17.9450 38.5649

REMARK 3 T TENSOR

REMARK 3 Ti l 0.1810 T22: 0.0978

REMARK 3 T33 0.0232 T12: 0.0341

REMARK 3 T13 0.0557 T23: 0.0304

REMARK 3 L TENSOR

REMARK 3 Ll l 0.2319 L22: 0.4289

REMARK 3 L33 0.1117 L12: -0.1966

REMARK 3 L13 -0.1806 L23: 0.1427

REMARK 3 S TENSOR

REMARK 3 Sl l -0.0686 S12: -0.0808 S13: -0.0932

REMARK 3 S21 0.3166 S22: 0.0367 S23: 0.1793

REMARK 3 S31 -0.0491 S32: 0.0105 S33: 0.0128

REMARK 3 TLS GROUP : 8

REMARK 3 SELECTION: (chain A and resid 745:784)

REMARK 3 ORIGIN FOR THE GROUP (A): -11.6858 22.3339 40.0086

REMARK 3 T TENSOR

REMARK 3 Ti l 0.2287 T22: 0.1545

REMARK 3 T33 0.0630 T12: 0.0149

REMARK 3 T13 -0.0435 T23: -0.0560

REMARK 3 L TENSOR

REMARK 3 Ll l 0.7245 L22: 0.2836 REMARK 3 L33 0.1737 L12: 0.2671

REMARK 3 L13 0.2683 L23: -0.0868

REMARK 3 S TENSOR

REMARK 3 Sl l -0.0057 S12: -0.2615 S13: 0.1486

REMARK 3 S21 0.4585 S22: 0.1043 S23: 0.0595

REMARK 3 S31 0.0553 S32: -0.1127 S33: -0.0374

REMARK 3 TLS GROUP : 9

REMARK 3 SELECTION: (chain A and resid 785: 1007)

REMARK 3 ORIGIN FOR THE GROUP (A): -22.6107 31.0945 22.1110

REMARK 3 T TENSOR

REMARK 3 Ti l 0.0673 T22: 0.0143

REMARK 3 T33 -0.0550 T12: 0.0181

REMARK 3 T13 0.0317 T23: -0.0340

REMARK 3 L TENSOR

REMARK 3 Ll l 0.1531 L22: 0.2420

REMARK 3 L33 0.1748 L12: -0.2049

REMARK 3 L13 0.0436 L23: -0.0385

REMARK 3 S TENSOR

REMARK 3 Sl l 0.0402 S 12: 0.0182 S13: 0.1564

REMARK 3 S21 0.0508 S22: 0.0099 S23: 0.1717

REMARK 3 S31 -0.0277 S32: -0.0112 S33: 0.0603

REMARK 3 TLS GROUP : 10

REMARK 3 SELECTION: (chain A and resid 1008: 1028)

REMARK 3 ORIGIN FOR THE GROUP (A): -41.7133 13.2739 -4.6495

REMARK 3 T TENSOR

REMARK 3 Ti l 0.1607 T22: 0.1542

REMARK 3 T33 0.1038 T12: -0.0078

REMARK 3 T13 -0.1075 T23: -0.0331

REMARK 3 L TENSOR

REMARK 3 Ll l 0.1166 L22: 0.1450

REMARK 3 L33 0.0860 L12: -0.0011

REMARK 3 L13 0.0949 L23: 0.0627

REMARK 3 S TENSOR

REMARK 3 Sl l 0.0280 S12: 0.0026 S13: -0.0548

REMARK 3 S21 -0.0291 S22: -0.0405 S23: 0.1272

REMARK 3 S31 0.0483 S32: -0.1035 S33: -0.0183

REMARK 3 TLS GROUP : 11

REMARK 3 SELECTION: (chain B and resid 1:30)

REMARK 3 ORIGIN FOR THE GROUP (A): -12.1845 29.8696 4.3779

REMARK 3 T TENSOR

REMARK 3 Ti l 0.1333 T22: 0.1040

REMARK 3 T33 0.1013 T12: 0.0136

REMARK 3 T13 0.0294 T23: 0.0105

REMARK 3 L TENSOR

REMARK 3 Ll l 0.1085 L22: 0.0503

REMARK 3 L33 0.0397 L12: 0.0287 REMARK 3 L13: 0.0380 L23: -0.0019

REMARK 3 S TENSOR

REMARK 3 Sl l 0.0614 S12: 0.0237 S13: 0.2344

REMARK 3 S21 -0.1387 S22: -0.0933 S23: -0.0980

REMARK 3 S31 0.0049 S32: 0.0297 S33: -0.0198

REMARK 3 TLS GROUP : 12

REMARK 3 SELECTION: (chain C and resid 336:455)

REMARK 3 ORIGIN FOR THE GROUP (A): 18.1156 -28.8142 2.7882

REMARK 3 T TENSOR

REMARK 3 Ti l 0.1161 T22 0.1581

REMARK 3 T33 0.0277 T12 0.0206

REMARK 3 T13 0.0184 T23 0.0251

REMARK 3 L TENSOR

REMARK 3 Ll l 0.0445 L22: 0.5090

REMARK 3 L33 0.6220 L12: -0.2297

REMARK 3 L13 -0.0467 L23: -0.0863

REMARK 3 S TENSOR

REMARK 3 Sl l -0.0720 S12: -0.0594 S13: 0.0055

REMARK 3 S21 0.0626 S22: 0.0406 S23: -0.1057

REMARK 3 S31 0.0226 S32: 0.3415 S33: 0.0483

REMARK 3 TLS GROUP : 13

REMARK 3 SELECTION: (chain C and resid 456:514)

REMARK 3 ORIGIN FOR THE GROUP (A): 5.7839 -33.2533 24.4817

REMARK 3 T TENSOR

REMARK 3 Ti l 0.0965 T22: -0.1816

REMARK 3 T33 -0.2988 T12: 0.1152

REMARK 3 T13 -0.0727 T23: 0.3398

REMARK 3 L TENSOR

REMARK 3 Ll l 0.0728 L22 0.0824

REMARK 3 L33 0.0152 L12 -0.0411

REMARK 3 L13 0.1114 L23 0.0222

REMARK 3 S TENSOR

REMARK 3 Sl l -0.1784 S12: -0.1912 S13 0.2454

REMARK 3 S21 -0.0455 S22: 0.1529 S23: -0.4030

REMARK 3 S31 0.1257 S32: 0.0169 S33: 0.0246

REMARK 3 TLS GROUP : 14

REMARK 3 SELECTION: (chain C and resid 515:712)

REMARK 3 ORIGIN FOR THE GROUP (A): 5.2596 -5.4855 24.9155

REMARK 3 T TENSOR

REMARK 3 Ti l 0.0552 T22: 0.0474

REMARK 3 T33 0.0674 T12: 0.0046

REMARK 3 T13 -0.0171 T23: 0.0335

REMARK 3 L TENSOR

REMARK 3 Ll l 0.2949 L22: 0.5859

REMARK 3 L33 0.1329 L12: 0.0396

REMARK 3 L13 -0.0430 L23: -0.0838 REMARK 3 S TENSOR

REMARK 3 Sl l -0.0109 S12: -0.0023 S13: 0.0634

REMARK 3 S21 0.0012 S22: -0.0438 S23: -0.1795

REMARK 3 S31 0.0034 S32: 0.0307 S33: 0.0469

REMARK 3 TLS GROUP : 15

REMARK 3 SELECTION: (chain C and resid 713:718)

REMARK 3 ORIGIN FOR THE GROUP (A): -41.7038 -18.6909 20.9117

REMARK 3 T TENSOR

REMARK 3 Ti l 0.3191 T22: 0.2879

REMARK 3 T33 0.4346 T12: 0.1063

REMARK 3 T13 -0.2312 T23: 0.1756

REMARK 3 L TENSOR

REMARK 3 Ll l 0.8180 L22: 0.5528

REMARK 3 L33 0.1707 L12: -0.2306

REMARK 3 L13 -0.3461 L23: 0.1540

REMARK 3 S TENSOR

REMARK 3 Sl l -0.0693 S12: 0.0774 S13: 0.0012

REMARK 3 S21 0.2600 S22: 0.0268 S23: 0.0123

REMARK 3 S31 0.0328 S32: 0.0101 S33: 0.0446

REMARK 3 TLS GROUP : 16

REMARK 3 SELECTION: (chain C and resid 719:744)

REMARK 3 ORIGIN FOR THE GROUP (A): -36.2846 -6.7400 21.6644

REMARK 3 T TENSOR

REMARK 3 Ti l 0.0856 T22: 0.0933

REMARK 3 T33 0.1325 T12: 0.0273

REMARK 3 T13 0.0609 T23: 0.0254

REMARK 3 L TENSOR

REMARK 3 Ll l 0.1109 L22: 0.0986

REMARK 3 L33 0.1361 L12: -0.0977

REMARK 3 L13 -0.1274 L23: 0.0408

REMARK 3 S TENSOR

REMARK 3 Sl l -0.0107 S12: 0.0295 S13: -0.0133

REMARK 3 S21 0.1919 S22: 0.0304 S23: 0.2829

REMARK 3 S31 -0.0340 S32: -0.0676 S33: -0.0059

REMARK 3 TLS GROUP : 17

REMARK 3 SELECTION: (chain C and resid 745:763)

REMARK 3 ORIGIN FOR THE GROUP (A): -33.7611 -5.0786 33.1546

REMARK 3 T TENSOR

REMARK 3 Ti l 0.2879 T22: 0.3843

REMARK 3 T33 0.4064 T12: 0.0006

REMARK 3 T13 0.0841 T23: -0.0296

REMARK 3 L TENSOR

REMARK 3 Ll l 0.2954 L22: 0.7779

REMARK 3 L33 0.1057 L12: -0.1818

REMARK 3 L13 0.0643 L23: -0.2878

REMARK 3 S TENSOR REMARK 3 Sl l: -0.0900 S12: -0.0743 S13: -0.0217

REMARK 3 S21: 0.0865 S22: -0.0228 S23: 0.0270

REMARK 3 S31: -0.0636 S32: -0.1123 S33: 0.0642

REMARK 3 TLS GROUP : 18

REMARK 3 SELECTION: (chain C and resid 764:784)

REMARK 3 ORIGIN FOR THE GROUP (A): -39.3518 -12.4108 12.7967

REMARK 3 T TENSOR

REMARK 3 Ti l 0.0965 T22: 0.1475

REMARK 3 T33 0.2151 T12: -0.0410

REMARK 3 T13 -0.0656 T23: 0.0785

REMARK 3 L TENSOR

REMARK 3 Ll l 0.5169 L22 0.2927

REMARK 3 L33 0.3058 L12 0.0661

REMARK 3 L13 0.2746 L23 -0.1184

REMARK 3 S TENSOR

REMARK 3 Sl l 0.0383 S12 -0.0743 S13: 0.0343

REMARK 3 S21 0.0399 S22 0.1625 S23: 0.4053

REMARK 3 S31 0.0938 S32 -0.2951 S33: 0.0007

REMARK 3 TLS GROUP : 19

REMARK 3 SELECTION: (chain C and resid 785: 1026)

REMARK 3 ORIGIN FOR THE GROUP (A): -16.7621 -18.2996 26.3229

REMARK 3 T TENSOR

REMARK 3 Ti l 0.0871 T22: 0.0174

REMARK 3 T33 -0.0467 T12: -0.0138

REMARK 3 T13 0.0215 T23: 0.0416

REMARK 3 L TENSOR

REMARK 3 Ll l 0.3701 L22 0.2520

REMARK 3 L33 0.1600 L12 -0.1091

REMARK 3 L13 0.0210 L23 0.0529

REMARK 3 S TENSOR

REMARK 3 Sl l: -0.0167 S12: -0.0095 S13: -0.0262

REMARK 3 S21: 0.0675 S22: -0.0416 S23: 0.0828

REMARK 3 S31: 0.0427 S32: -0.0165 S33: -0.1420

REMARK 3 TLS GROUP : 20

REMARK 3 SELECTION: (chain C and resid 1027: 1126)

REMARK 3 ORIGIN FOR THE GROUP (A): 1.6383 -7.4935 45.6048

REMARK 3 T TENSOR

REMARK 3 Ti l: 0.1552 T22: 0.4766

REMARK 3 T33: 0.2434 T12: 0.0628

REMARK 3 T13: -0.0455 T23: -0.0627

REMARK 3 L TENSOR

REMARK 3 Ll l: 0.2042 L22: 0.1783

REMARK 3 L33: 0.1360 L12: -0.1819

REMARK 3 L13: -0.0380 L23: 0.0504

REMARK 3 S TENSOR

REMARK 3 Sl l: -0.0177 S12: -0.0430 S13: 0.0255 REMARK S21: 0.0498 S22: -0.0469 S23: -0.0111

REMARK S31: 0.0870 S32: -0.0054 S33: 0.0237

REMARK TLS GROUP : 21

REMARK SELECTION: (chain D and resid 1:30)

REMARK ORIGIN FOR THE GROUP (A): -2.9791 -18.6567 12.4998

REMARK T TENSOR

REMARK Ti l 0.1454 T22 0.0846

REMARK T33 0.0147 T12 0.0191

REMARK T13 0.0098 T23 0.0190

REMARK L TENSOR

REMARK Ll l 0.1028 L22 0.0369

REMARK L33 0.1355 L12 -0.0440

REMARK L13 0.0141 L23 -0.0116

REMARK S TENSOR

REMARK Sl l 0.0239 S12: 0.0129 S13: 0.0681

REMARK S21 -0.1045 S22: -0.0629 S23: -0.0861

REMARK S31 0.2361 S32: 0.0166 S33: 0.0167

REMARK

REMARK NCS DETAILS.

REMARK NUMBER OF NCS GROUPS : 2

REMARK NCS GROUP : 1

REMARK NCS OPERATOR : 1

REMARK REFERENCE SELECTION: chain A and (resseq 315:619 or

REMARK : resseq 621:633 or resseq 635:714

REMARK : or resseq 719:746 or resseq

REMARK : 762: 1028 or resseq 1212: 1212 )

REMARK SELECTION : chain C and (resseq 336:619 or

REMARK : resseq 621:633 or resseq 635:714

REMARK : or resseq 719:746 or resseq

REMARK : 762: 1028 or resseq 1212: 1212 )

REMARK ATOM PAIRS NUMBER : 5385

REMARK RMSD : 0.025

REMARK NCS GROUP : 2

REMARK NCS OPERATOR : 1

REMARK REFERENCE SELECTION: chain B and (resseq 13:26 )

REMARK SELECTION : chain D and (resseq 13:26 )

REMARK ATOM PAIRS NUMBER : 95

REMARK RMSD : 0.017

REMARK 3

CRYST1 98.580 136.660 153.538 90.00 102.90 90.00 1 1 2 1

SCALE 1 0.010144 0.000000 0.002324 0.00000

SCALE2 0.000000 0.007317 0.000000 0.00000

SCALE3 0.000000 0.000000 0.006682 0.00000

ATOM 1 N THR A 315 -3.950 43.451 -42.729 1.00 63.41 N

ANISOU 1 N THR A 315 8898 7782 7412 48 -544 1438 N

ATOM 2 CA THR A 315 -5.238 43.853 -43.285 1.00 67.61 C ANISOU 2 CA THR A 315 9417 8304 7968 61 -640 1421 C

ATOM 3 CB THR A 315 -5.068 44.706 -44.563 1.00 75.08 C

ANISOU 3 CB THR A 315 10477 9157 8894 47 -714 1419 C

ATOM 4 0G1 THR A 315 -6.355 45.111 -45.048 1.00 75.34 O

ANISOU 4 0G1 THR A 315 10491 9182 8953 62 -809 1402 O

ATOM 5 CG2 THR A 315 -4.336 43.923 -45.647 1.00 77.52 C

ANISOU 5 CG2 THR A 315 10897 9397 9159 -19 -683 1457 C

ATOM 6 C THR A 315 -6.116 42.635 -43.567 1.00 54.19 C

ANISOU 6 C THR A 315 7686 6624 6278 20 -642 1442 C

ATOM 7 O THR A 315 -7.305 42.627 -43.242 1.00 47.72 O

ANISOU 7 O THR A 315 6783 5853 5498 44 -686 1432 O

ATOM 8 N HIS A 316 -5.529 41.606 -44.171 1.00 50.55 N

ANISOU 8 N HIS A 316 7294 6128 5784 -41 -594 1476 N

ATOM 9 CA HIS A 316 -6.226 40.333 -44.322 1.00 50.20 C

ANISOU 9 CA HIS A 316 7220 6104 5748 -84 -587 1499 C

ATOM 10 CB HIS A 316 -5.542 39.442 -45.361 1.00 46.95 C

ANISOU 10 CB HIS A 316 6927 5623 5289 -149 -559 1533 C

ATOM 11 CG HIS A 316 -6.185 38.099 -45.517 1.00 48.94 C

ANISOU 11 CG HIS A 316 7158 5890 5547 -195 -554 1557 C

ATOM 12 CD2 HIS A 316 -5.663 36.891 -45.842 1.00 49.35 C

ANISOU 12 CD2 HIS A 316 7265 5921 5566 -247 -498 1589 C

ATOM 13 ND1 HIS A 316 -7.537 37.895 -45.337 1.00 53.91 N

ANISOU 13 ND1 HIS A 316 7702 6558 6223 -191 -615 1553 N

ATOM 14 CE1 HIS A 316 -7.819 36.619 -45.534 1.00 50.89 C

ANISOU 14 CE1 HIS A 316 7320 6177 5839 -241 -600 1582 C

ATOM 15 NE2 HIS A 316 -6.700 35.989 -45.843 1.00 51.61 N

ANISOU 15 NE2 HIS A 316 7498 6231 5879 -275 -530 1602 N

ATOM 16 C HIS A 316 -6.274 39.639 -42.965 1.00 32.40 C

ANISOU 16 C HIS A 316 4848 3945 3518 -66 -510 1502 C

ATOM 17 O HIS A 316 -7.301 39.086 -42.571 1.00 24.86 O

ANISOU 17 O HIS A 316 3804 3044 2599 -64 -525 1507 O

ATOM 18 N ALA A 317 -5.157 39.681 -42.249 1.00 22.49 N

ANISOU 18 N ALA A 317 3590 2710 2244 -53 -428 1502 N

ATOM 19 CA ALA A 317 -5.137 39.210 -40.873 1.00 25.98 C

ANISOU 19 CA ALA A 317 3920 3244 2708 -25 -355 1500 C

ATOM 20 CB ALA A 317 -3.758 39.377 -40.275 1.00 36.47 C

ANISOU 20 CB ALA A 317 5270 4576 4010 -15 -273 1500 C

ATOM 21 C ALA A 317 -6.169 39.981 -40.059 1.00 27.33 C

ANISOU 21 C ALA A 317 3982 3479 2924 44 -402 1469 C

ATOM 22 O ALA A 317 -6.811 39.424 -39.171 1.00 34.29 O

ANISOU 22 O ALA A 317 4755 4438 3834 63 -374 1473 O

ATOM 23 N ASP A 318 -6.326 41.266 -40.373 1.00 29.53 N

ANISOU 23 N ASP A 318 4291 3722 3206 82 -474 1441 N

ATOM 24 CA ASP A 318 -7.318 42.112 -39.714 1.00 34.46 C

ANISOU 24 CA ASP A 318 4826 4399 3868 153 -526 1412 C

ATOM 25 CB ASP A 318 -7.179 43.566 -40.178 1.00 38.36 C ANISOU 25 CB ASP A 318 5383 4837 4356 189 -600 1382 C

ATOM 26 CG ASP A 318 -6.204 44.354 -39.334 1.00 51.73 C

ANISOU 26 CG ASP A 318 7077 6542 6037 236 -562 1359 C

ATOM 27 0D1 ASP A 318 -6.148 44.104 -38.111 1.00 67.43 O

ANISOU 27 OD1 ASP A 318 8979 8605 8037 275 -504 1352 O

ATOM 28 OD2 ASP A 318 -5.499 45.225 -39.886 1.00 53.10 O

ANISOU 28 OD2 ASP A 318 7338 6648 6191 235 -593 1350 O

ATOM 29 C ASP A 318 -8.744 41.626 -39.957 1.00 31.61 C

ANISOU 29 C ASP A 318 4401 4066 3544 146 -579 1425 C

ATOM 30 O ASP A 318 -9.543 41.525 -39.022 1.00 39.34 O

ANISOU 30 O ASP A 318 5263 5126 4558 192 -571 1422 O

ATOM 31 N ASER A 319 -9.063 41.328 -41.214 0.50 32.02 N

ANISOU 31 N ASER A 319 4528 4051 3588 89 -636 1442 N

ATOM 32 CA ASER A 319 -10.403 40.860 -41.561 0.50 34.88 C

ANISOU 32 CA ASER A 319 4837 4428 3986 74 -696 1459 C

ATOM 33 CB ASER A 319 -10.610 40.852 -43.081 0.50 34.47 C

ANISOU 33 CB ASER A 319 4897 4282 3918 18 -774 1469 C

ATOM 34 OG ASER A 319 -9.691 39.986 -43.724 0.50 36.39 O

ANISOU 34 OG ASER A 319 5237 4471 4118 -47 -728 1492 O

ATOM 35 C ASER A 319 -10.668 39.476 -40.978 0.50 36.23 C

ANISOU 35 C ASER A 319 4930 4660 4175 43 -635 1492 C

ATOM 36 O ASER A 319 -11.799 39.152 -40.608 0.50 36.92 O

ANISOU 36 O ASER A 319 4917 4804 4308 57 -661 1506 O

ATOM 37 N BSER A 319 -9.060 41.330 -41.214 0.50 31.99 N

ANISOU 37 N BSER A 319 4525 4047 3584 89 -635 1442 N

ATOM 38 CA BSER A 319 -10.395 40.859 -41.571 0.50 34.91 C

ANISOU 38 CA BSER A 319 4843 4432 3991 73 -696 1459 C

ATOM 39 CB BSER A 319 -10.575 40.832 -43.092 0.50 34.53 C

ANISOU 39 CB BSER A 319 4908 4289 3925 17 -772 1469 C

ATOM 40 OG BSER A 319 -10.439 42.132 -43.644 0.50 27.87 O

ANISOU 40 OG BSER A 319 4129 3390 3069 46 -835 1440 O

ATOM 41 C BSER A 319 -10.665 39.480 -40.977 0.50 36.23 C

ANISOU 41 C BSER A 319 4930 4660 4175 43 -635 1492 C

ATOM 42 0 BSER A 319 -11.795 39.165 -40.599 0.50 37.06 O

ANISOU 42 O BSER A 319 4934 4821 4325 58 -661 1506 O

ATOM 43 N LEU A 320 -9.623 38.660 -40.894 1.00 28.69 N

ANISOU 43 N LEU A 320 4019 3695 3186 1 -553 1507 N

ATOM 44 CA LEU A 320 -9.749 37.337 -40.295 1.00 29.65 C

ANISOU 44 CA LEU A 320 4071 3873 3321 -28 -488 1538 C

ATOM 45 CB LEU A 320 -8.478 36.511 -40.511 1.00 33.00 C

ANISOU 45 CB LEU A 320 4579 4262 3697 -81 -407 1555 C

ATOM 46 CG LEU A 320 -8.290 35.988 -41.940 1.00 39.64 C

ANISOU 46 CG LEU A 320 5549 5008 4504 -152 -445 1575 C

ATOM 47 CD1 LEU A 320 -6.895 35.416 -42.160 1.00 33.45 C

ANISOU 47 CD1 LEU A 320 4858 4186 3666 -190 -362 1590 C

ATOM 48 CD2 LEU A 320 -9.359 34.956 -42.276 1.00 44.32 C ANISOU 48 CD2 LEU A 320 6105 5608 5126 -197 -487 1605 C

ATOM 49 C LEU A 320 -10.090 37.466 -38.810 1.00 30.47 C

ANISOU 49 C LEU A 320 4036 4083 3459 39 -439 1529 C

ATOM 50 O LEU A 320 -10.975 36.771 -38.315 1.00 24.12 O

ANISOU 50 O LEU A 320 3130 3341 2694 40 -435 1553 O

ATOM 51 N ASN A 321 -9.400 38.366 -38.109 1.00 32.36 N

ANISOU 51 N ASN A 321 4272 4340 3684 97 -406 1498 N

ATOM 52 CA ASN A 321 -9.677 38.616 -36.691 1.00 28.66 C

ANISOU 52 CA ASN A 321 3681 3967 3240 171 -363 1485 C

ATOM 53 CB ASN A 321 -8.669 39.621 -36.110 1.00 35.89 C

ANISOU 53 CB ASN A 321 4629 4878 4128 224 -334 1449 C

ATOM 54 CG ASN A 321 -8.881 39.887 -34.618 1.00 30.87 C

ANISOU 54 CG ASN A 321 3879 4337 3511 307 -288 1432 C

ATOM 55 OD1 ASN A 321 -8.756 38.985 -33.789 1.00 30.47 O ANISOU 55 OD1 ASN A 321 3760 4350 3466 304 -211 1451 O

ATOM 56 ND2 ASN A 321 -9.178 41.140 -34.273 1.00 31.56 N ANISOU 56 ND2 ASN A 321 3952 4433 3605 383 -337 1397 N

ATOM 57 C ASN A 321 -11.109 39.118 -36.523 1.00 38.83 C

ANISOU 57 C ASN A 321 4881 5299 4576 223 -435 1482 C

ATOM 58 0 ASN A 321 -11.822 38.701 -35.609 1.00 36.18 O

ANISOU 58 O ASN A 321 4425 5048 4273 258 -407 1498 O

ATOM 59 N ASN A 322 -11.533 40.002 -37.421 1.00 33.55 N

ANISOU 59 N ASN A 322 4269 4571 3908 227 -527 1466 N

ATOM 60 CA ASN A 322 -12.913 40.481 -37.411 1.00 40.25 C

ANISOU 60 CA ASN A 322 5040 5451 4800 271 -602 1468 C

ATOM 61 CB ASN A 322 -13.146 41.512 -38.513 1.00 43.55 C

ANISOU 61 CB ASN A 322 5545 5790 5211 269 -701 1446 C

ATOM 62 CG ASN A 322 -14.582 41.994 -38.551 1.00 51.49 C

ANISOU 62 CG ASN A 322 6473 6828 6264 312 -781 1450 C

ATOM 63 OD1 ASN A 322 -15.171 42.298 -37.511 1.00 46.14 O ANISOU 63 OD1 ASN A 322 5685 6231 5613 388 -764 1447 O

ATOM 64 ND2 ASN A 322 -15.159 42.055 -39.749 1.00 48.82 N ANISOU 64 ND2 ASN A 322 6190 6425 5935 267 -867 1461 N

ATOM 65 C ASN A 322 -13.927 39.346 -37.556 1.00 30.41 C

ANISOU 65 C ASN A 322 3720 4239 3596 227 -614 1514 C

ATOM 66 O ASN A 322 -14.900 39.272 -36.806 1.00 37.56 O

ANISOU 66 O ASN A 322 4503 5224 4545 275 -616 1530 O

ATOM 67 N LEU A 323 -13.693 38.461 -38.522 1.00 29.47 N

ANISOU 67 N LEU A 323 3678 4057 3463 139 -625 1539 N

ATOM 68 CA LEU A 323 -14.578 37.318 -38.743 1.00 41.38 C

ANISOU 68 CA LEU A 323 5130 5585 5009 87 -643 1586 C

ATOM 69 CB LEU A 323 -14.124 36.506 -39.957 1.00 50.13 C

ANISOU 69 CB LEU A 323 6358 6602 6086 -8 -663 1604 C

ATOM 70 CG LEU A 323 -14.250 37.195 -41.318 1.00 55.10 C

ANISOU 70 CG LEU A 323 7104 7134 6698 -33 -759 1589 C

ATOM 71 CD1 LEU A 323 -13.673 36.312 -42.410 1.00 53.51 C ANISOU 71 CD1 LEU A 323 7028 6847 6458 -119 -763 1607 C

ATOM 72 CD2 LEU A 323 -15.703 37.545 -41.614 1.00 52.35 C

ANISOU 72 CD2 LEU A 323 6690 6797 6403 -17 -858 1602 C

ATOM 73 C LEU A 323 -14.637 36.427 -37.509 1.00 44.68 C

ANISOU 73 C LEU A 323 5429 6098 5449 103 -555 1611 C

ATOM 74 0 LEU A 323 -15.712 35.998 -37.092 1.00 26.38 O

ANISOU 74 O LEU A 323 2997 3843 3183 116 -570 1645 O

ATOM 75 N ALA A 324 -13.473 36.151 -36.930 1.00 33.33 N

ANISOU 75 N ALA A 324 4017 4673 3973 103 -462 1598 N

ATOM 76 CA ALA A 324 -13.397 35.394 -35.692 1.00 32.58 C

ANISOU 76 CA ALA A 324 3817 4670 3894 125 -371 1617 C

ATOM 77 CB ALA A 324 -11.938 35.326 -35.209 1.00 24.18 C

ANISOU 77 CB ALA A 324 2808 3600 2780 125 -279 1595 C

ATOM 78 C ALA A 324 -14.308 36.003 -34.615 1.00 28.83 C

ANISOU 78 C ALA A 324 3206 4288 3461 219 -373 1614 C

ATOM 79 0 ALA A 324 -15.119 35.301 -34.010 1.00 37.99 O

ANISOU 79 O ALA A 324 4249 5521 4663 227 -354 1652 O

ATOM 80 N ASN A 325 -14.156 37.304 -34.378 1.00 28.45 N

ANISOU 80 N ASN A 325 3175 4236 3397 291 -394 1571 N

ATOM 81 CA ASN A 325 -14.994 38.042 -33.430 1.00 34.71 C

ANISOU 81 CA ASN A 325 3857 5110 4221 391 -402 1564 C

ATOM 82 CB ASN A 325 -14.717 39.548 -33.524 1.00 29.81 C

ANISOU 82 CB ASN A 325 3297 4454 3575 456 -448 1511 C

ATOM 83 CG ASN A 325 -13.342 39.933 -33.008 1.00 40.72 C

ANISOU 83 CG ASN A 325 4742 5821 4908 475 -384 1473 C

ATOM 84 OD1 ASN A 325 -12.789 40.967 -33.394 1.00 47.96 O

ANISOU 84 OD1 ASN A 325 5746 6678 5796 493 -422 1435 O

ATOM 85 ND2 ASN A 325 -12.783 39.107 -32.132 1.00 28.34 N

ANISOU 85 ND2 ASN A 325 3130 4306 3332 471 -290 1486 N

ATOM 86 C ASN A 325 -16.481 37.803 -33.678 1.00 39.66 C

ANISOU 86 C ASN A 325 4393 5769 4906 392 -467 1605 C

ATOM 87 O ASN A 325 -17.248 37.556 -32.747 1.00 34.49 O

ANISOU 87 O ASN A 325 3609 5206 4290 445 -438 1632 O

ATOM 88 N ILE A 326 -16.883 37.890 -34.942 1.00 36.94 N

ANISOU 88 N ILE A 326 4118 5348 4570 335 -556 1612 N

ATOM 89 CA ILE A 326 -18.279 37.686 -35.321 1.00 49.06 C

ANISOU 89 CA ILE A 326 5578 6901 6162 326 -630 1654 C

ATOM 90 CB ILE A 326 -18.481 37.922 -36.829 1.00 42.46 C

ANISOU 90 CB ILE A 326 4851 5961 5322 260 -732 1650 C

ATOM 91 CG2 ILE A 326 -19.899 37.541 -37.242 1.00 48.56 C

ANISOU 91 CG2 ILE A 326 5546 6748 6158 238 -810 1700 C

ATOM 92 CGI ILE A 326 -18.188 39.384 -37.170 1.00 33.74 C

ANISOU 92 CGI ILE A 326 3823 4809 4186 312 -779 1596 C

ATOM 93 CD1 ILE A 326 -18.014 39.649 -38.654 1.00 34.62 C

ANISOU 93 CD1 ILE A 326 4071 4808 4276 246 -862 1583 C

ATOM 94 C ILE A 326 -18.773 36.287 -34.943 1.00 49.96 C ANISOU 94 C ILE A 326 5595 7069 6317 281 -592 1714 C

ATOM 95 O ILE A 326 19.759 36.139 -34.215 1.00 42.06 o

ANISOU 95 O ILE A 326 4461 6154 5367 329 -587 1750 o

ATOM 96 N LYS A 327 --18.083 35.265 -35.438 1.00 52.14 N

ANISOU 96 N LYS A 327 5943 7297 6571 192 -565 1726 N

ATOM 97 CA LYS A 327 -18.439 33.886 -35.125 1.00 61.20 C

ANISOU 97 CA LYS A 327 7012 8487 7752 142 -529 1782 C

ATOM 98 CB LYS A 327 -17.495 32.910 -35.832 1.00 66.27 C

ANISOU 98 CB LYS A 327 7768 9056 8355 45 -505 1785 C

ATOM 99 CG LYS A 327 -18.116 32.210 -37.030 1.00 71.64 C

ANISOU 99 CG LYS A 327 8496 9666 9057 -43 -593 1821 C

ATOM 100 CD LYS A 327 -18.812 33.197 -37.951 1.00 75.38 C

ANISOU 100 CD LYS A 327 9012 10085 9543 -32 -705 1807 C

ATOM 101 CE LYS A 327 -19.485 32.482 -39.109 1.00 81.58 C

ANISOU 101 CE LYS A 327 9843 10801 10353 -119 -798 1845 C

ATOM 102 NZ LYS A 327 -20.436 31.438 -38.636 1.00 86.58 N

ANISOU 102 NZ LYS A 327 10348 11497 11053 -143 -801 1910 N

ATOM 103 C LYS A 327 -18.428 33.647 -33.617 1.00 60.23 C

ANISOU 103 C LYS A 327 6762 8478 7645 210 -431 1794 C

ATOM 104 O LYS A 327 -19.204 32.840 -33.100 1.00 58.94 o

ANISOU 104 O LYS A 327 6481 8381 7532 206 -415 1847 o

ATOM 105 N ARG A 328 -17.549 34.356 -32.916 1.00 52.78 N

ANISOU 105 N ARG A 328 5843 7553 6657 274 -369 1746 N

ATOM 106 CA ARG A 328 -17.494 34.274 -31.464 1.00 50.36 C

ANISOU 106 CA ARG A 328 5426 7350 6357 350 -279 1749 C

ATOM 107 CB ARG A 328 -16.308 35.073 -30.920 1.00 47.58 C

ANISOU 107 CB ARG A 328 5139 6991 5948 403 -223 1690 C

ATOM 108 CG ARG A 328 -16.211 35.047 -29.405 1.00 50.52 C

ANISOU 108 CG ARG A 328 5407 7466 6321 488 -132 1689 C

ATOM 109 CD ARG A 328 -15.076 35.913 -28.890 1.00 61.49 C

ANISOU 109 CD ARG A 328 6865 8842 7655 541 -90 1629 C

ATOM 110 NE ARG A 328 -14.881 35.728 -27.454 1.00 79.04 N

ANISOU 110 NE ARG A 328 8999 11159 9875 614 1 1629 N

ATOM 111 CZ ARG A 328 -13.912 36.298 -26.746 1.00 91.49 C

ANISOU 111 CZ ARG A 328 10614 12740 11409 665 50 1585 C

ATOM 112 NH1 ARG A 328 -13.034 37.097 -27.339 1.00 98.03 N

ANISOU 112 NH1 ARG A 328 11565 13486 12197 650 18 1539 N

ATOM 113 NH2 ARG A 328 -13.818 36.066 -25.444 1.00 91.90 N

ANISOU 113 NH2 ARG A 328 10582 12879 11459 732 131 1588 N

ATOM 114 C ARG A 328 18.797 34.789 -30.859 1.00 40.25 C

ANISOU 114 C ARG A 328 4013 6150 5129 435 -309 1774 C

ATOM 115 O ARG A 328 19.431 34.111 -30.051 1.00 38.74 o

ANISOU 115 O ARG A 328 3694 6045 4979 458 -266 1822 o

ATOM 116 N GLU A 329 19.189 35.994 -31.259 1.00 38.38 N

ANISOU 116 N GLU A 329 3807 5885 4890 484 -381 1744 N

ATOM 117 CA GLU A 329 -20.420 36.601 -30.765 1.00 55.79 C ANISOU 117 CA GLU A 329 5896 8160 7140 571 -415 1766 C

ATOM 118 CB GLU A 329 -20.598 38.007 -31.343 1.00 63.15 C ANISOU 118 CB GLU A 329 6896 9041 8056 617 -496 1721 C

ATOM 119 CG GLU A 329 -19.480 38.968 -30.971 1.00 70.77 C ANISOU 119 CG GLU A 329 7949 9983 8959 671 -462 1651 C

ATOM 120 CD GLU A 329 -19.342 39.146 -29.470 1.00 75.22 C ANISOU 120 CD GLU A 329 8424 10642 9512 774 -376 1642 C ATOM 121 OE1 GLU A 329 -20.272 39.702 -28.847 1.00 70.34 O ANISOU 121 OE1 GLU A 329 7711 10093 8920 868 -388 1654 O ATOM 122 OE2 GLU A 329 -18.303 38.731 -28.913 1.00 75.54 O ANISOU 122 OE2 GLU A 329 8494 10691 9519 763 -296 1624 O

ATOM 123 C GLU A 329 -21.633 35.734 -31.089 1.00 65.45 C

ANISOU 123 C GLU A 329 7024 9410 8434 525 -458 1840 C

ATOM 124 O GLU A 329 -22.570 35.645 -30.296 1.00 67.49 O

ANISOU 124 O GLU A 329 7145 9761 8739 588 -441 1884 O

ATOM 125 N GLN A 330 -21.607 35.096 -32.257 1.00 64.24 N

ANISOU 125 N GLN A 330 6946 9175 8287 416 -516 1857 N

ATOM 126 CA GLN A 330 -22.661 34.167 -32.653 1.00 56.67 C ANISOU 126 CA GLN A 330 5910 8226 7394 355 -565 1929 C

ATOM 127 CB GLN A 330 -22.396 33.613 -34.056 1.00 49.30 C ANISOU 127 CB GLN A 330 5102 7180 6449 236 -635 1931 C

ATOM 128 CG GLN A 330 -22.613 34.604 -35.189 1.00 49.04 C ANISOU 128 CG GLN A 330 5167 7062 6404 229 -739 1898 C

ATOM 129 CD GLN A 330 -22.260 34.011 -36.542 1.00 72.34 C ANISOU 129 CD GLN A 330 8250 9901 9336 116 -800 1898 C ATOM 130 OE1 GLN A 330 -21.899 32.838 -36.641 1.00 77.16 O ANISOU 130 OE1 GLN A 330 8878 10497 9943 44 -769 1924 O ATOM 131 NE2 GLN A 330 -22.357 34.821 -37.591 1.00 77.76 N ANISOU 131 NE2 GLN A 330 9034 10506 10005 105 -888 1868 N

ATOM 132 C GLN A 330 -22.770 33.016 -31.655 1.00 70.16 C

ANISOU 132 C GLN A 330 7502 10022 9133 352 -480 1981 C

ATOM 133 O GLN A 330 -23.827 32.399 -31.516 1.00 76.16 O

ANISOU 133 O GLN A 330 8147 10831 9960 340 -504 2050 O

ATOM 134 N GLY A 331 -21.671 32.735 -30.962 1.00 63.74 N

ANISOU 134 N GLY A 331 6718 9229 8273 361 -382 1951 N

ATOM 135 CA GLY A 331 -21.632 31.650 -30.001 1.00 68.27 C ANISOU 135 CA GLY A 331 7191 9881 8867 358 -294 1994 C

ATOM 136 C GLY A 331 -20.848 30.467 -30.532 1.00 68.33 C

ANISOU 136 C GLY A 331 7278 9829 8853 246 -271 2002 C

ATOM 137 O GLY A 331 -20.586 29.506 -29.806 1.00 67.92 O

ANISOU 137 O GLY A 331 7167 9830 8808 232 -193 2030 O

ATOM 138 N ASN A 332 -20.479 30.539 -31.808 1.00 59.08 N

ANISOU 138 N ASN A 332 6245 8549 7655 170 -341 1978 N

ATOM 139 CA ASN A 332 -19.684 29.494 -32.441 1.00 59.63 C ANISOU 139 CA ASN A 332 6411 8550 7695 68 -326 1981 C

ATOM 140 CB ASN A 332 -19.891 29.511 -33.957 1.00 64.74 C ANISOU 140 CB ASN A 332 7175 9086 8339 -12 -435 1980 C

ATOM 141 CG ASN A 332 -19.320 28.282 -34.640 1.00 68.92 C ANISOU 141 CG ASN A 332 7792 9547 8846 -118 -431 1997 C

ATOM 142 OD1 ASN A 332 -18.690 27.433 -34.003 1.00 60.14 O ANISOU 142 OD1 ASN A 332 6660 8470 7720 -135 -343 2007 O

ATOM 143 ND2 ASN A 332 -19.541 28.178 -35.948 1.00 71.30 N ANISOU 143 ND2 ASN A 332 8194 9751 9144 -187 -527 2001 N

ATOM 144 C ASN A 332 -18.205 29.660 -32.101 1.00 62.14 C

ANISOU 144 C ASN A 332 6820 8850 7939 79 -238 1925 C

ATOM 145 O ASN A 332 -17.454 30.310 -32.829 1.00 53.84 O

ANISOU 145 O ASN A 332 5900 7720 6838 66 -262 1877 O

ATOM 146 N ILE A 333 -17.792 29.064 -30.989 1.00 60.03 N

ANISOU 146 N ILE A 333 6481 8659 7670 103 -136 1936 N

ATOM 147 CA ILE A 333 -16.447 29.272 -30.472 1.00 44.93 C

ANISOU 147 CA ILE A 333 4634 6744 5695 126 -48 1887 C

ATOM 148 CB ILE A 333 -16.361 28.916 -28.977 1.00 49.06 C

ANISOU 148 CB ILE A 333 5034 7377 6228 189 56 1901 C

ATOM 149 CG2 ILE A 333 -14.973 29.207 -28.440 1.00 54.02 C

ANISOU 149 CG2 ILE A 333 5732 8001 6794 214 141 1850 C

ATOM 150 CGI ILE A 333 -17.409 29.703 -28.187 1.00 48.07 C

ANISOU 150 CGI ILE A 333 4783 7338 6144 293 42 1912 C

ATOM 151 CD1 ILE A 333 -17.361 31.200 -28.434 1.00 57.76 C

ANISOU 151 CD1 ILE A 333 6069 8532 7346 359 -9 1857 C

ATOM 152 C ILE A 333 -15.388 28.499 -31.255 1.00 44.81 C

ANISOU 152 C ILE A 333 4748 6644 5632 31 -29 1879 C

ATOM 153 0 ILE A 333 -14.264 28.972 -31.411 1.00 41.58 O ANISOU 153 O ILE A 333 4442 6190 5165 34 3 1832 O

ATOM 154 N GLU A 334 -15.739 27.315 -31.748 1.00 34.15 N

ANISOU 154 N GLU A 334 3395 5273 4307 -51 -50 1926 N

ATOM 155 CA GLU A 334 -14.792 26.526 -32.535 1.00 47.51 C

ANISOU 155 CA GLU A 334 5215 6883 5952 -138 -35 1921 C

ATOM 156 CB GLU A 334 -15.332 25.115 -32.788 1.00 53.92 C

ANISOU 156 CB GLU A 334 5992 7693 6800 -217 -51 1981 C

ATOM 157 CG GLU A 334 -15.381 24.260 -31.534 1.00 68.88 C

ANISOU 157 CG GLU A 334 7760 9687 8723 -200 41 2015 C

ATOM 158 CD GLU A 334 -14.059 24.257 -30.782 1.00 84.41 C ANISOU 158 CD GLU A 334 9760 11678 10634 -173 156 1978 C

ATOM 159 OE1 GLU A 334 -12.996 24.270 -31.438 1.00 85.75 O ANISOU 159 OE1 GLU A 334 10067 11771 10744 -211 169 1947 O

ATOM 160 OE2 GLU A 334 -14.083 24.240 -29.533 1.00 86.98 O ANISOU 160 OE2 GLU A 334 9974 12099 10975 -111 232 1984 O

ATOM 161 C GLU A 334 -14.391 27.212 -33.850 1.00 43.57 C

ANISOU 161 C GLU A 334 4871 6273 5410 -170 -108 1886 C

ATOM 162 O GLU A 334 -13.213 27.234 -34.215 1.00 34.99 O

ANISOU 162 O GLU A 334 3901 5129 4263 -194 -69 1856 O

ATOM 163 N GLU A 335 -15.368 27.773 -34.556 1.00 45.65 N ANISOU 163 N GLU A 335 6325 5633 5388 -234 -1756 1722 N

ATOM 164 CA GLU A 335 -15.086 28.537 -35.772 1.00 56.07 C

ANISOU 164 CA GLU A 335 7711 6927 6666 -263 -1707 1686 C

ATOM 165 CB GLU A 335 -16.382 28.920 -36.492 1.00 61.83 C

ANISOU 165 CB GLU A 335 8471 7590 7430 -337 -1774 1819 C

ATOM 166 CG GLU A 335 -16.790 27.953 -37.590 1.00 76.28 C

ANISOU 166 CG GLU A 335 10445 9333 9204 -377 -1906 1863 C

ATOM 167 CD GLU A 335 -15.807 27.935 -38.747 1.00 90.75 C ANISOU 167 CD GLU A 335 12392 11141 10947 -369 -1869 1753 C

ATOM 168 OE1 GLU A 335 -15.008 28.887 -38.867 1.00 96.32 O ANISOU 168 OE1 GLU A 335 13060 11895 11643 -345 -1747 1668 O

ATOM 169 OE2 GLU A 335 -15.836 26.970 -39.539 1.00 96.34 O ANISOU 169 OE2 GLU A 335 13234 11779 11592 -391 -1959 1753 O

ATOM 170 C GLU A 335 -14.261 29.789 -35.475 1.00 50.42 C

ANISOU 170 C GLU A 335 6912 6291 5953 -247 -1549 1596 C

ATOM 171 O GLU A 335 -13.318 30.112 -36.206 1.00 40.98 O

ANISOU 171 O GLU A 335 5766 5107 4697 -232 -1484 1498 O

ATOM 172 N ALA A 336 -14.633 30.495 -34.410 1.00 44.81 N

ANISOU 172 N ALA A 336 6084 5633 5310 -255 -1485 1631 N

ATOM 173 CA ALA A 336 -13.875 31.653 -33.948 1.00 52.40 C

ANISOU 173 CA ALA A 336 6966 6673 6270 -251 -1329 1546 C

ATOM 174 CB ALA A 336 -14.468 32.192 -32.651 1.00 46.78 C

ANISOU 174 CB ALA A 336 6138 6003 5634 -268 -1276 1601 C

ATOM 175 C ALA A 336 -12.397 31.305 -33.758 1.00 50.14 C

ANISOU 175 C ALA A 336 6677 6461 5912 -200 -1277 1407 C

ATOM 176 O ALA A 336 -11.519 32.008 -34.254 1.00 29.06 O

ANISOU 176 O ALA A 336 4019 3826 3197 -198 -1181 1314 O

ATOM 177 N VAL A 337 -12.131 30.219 -33.035 1.00 50.14 N

ANISOU 177 N VAL A 337 6657 6490 5904 -157 -1339 1399 N

ATOM 178 CA VAL A 337 -10.763 29.763 -32.806 1.00 44.45 C

ANISOU 178 CA VAL A 337 5924 5845 5120 -100 -1297 1289 C

ATOM 179 CB VAL A 337 -10.722 28.501 -31.916 1.00 46.85 C

ANISOU 179 CB VAL A 337 6198 6171 5432 -52 -1377 1313 C

ATOM 180 CGI VAL A 337 -9.323 27.906 -31.893 1.00 37.85 C

ANISOU 180 CGI VAL A 337 5057 5097 4225 17 -1341 1218 C

ATOM 181 CG2 VAL A 337 -11.191 28.825 -30.506 1.00 41.75 C

ANISOU 181 CG2 VAL A 337 5427 5590 4845 -74 -1353 1357 C

ATOM 182 C VAL A 337 -10.058 29.464 -34.126 1.00 43.80 C

ANISOU 182 C VAL A 337 5958 5716 4967 -75 -1303 1225 C

ATOM 183 O VAL A 337 -8.914 29.872 -34.340 1.00 40.41 O

ANISOU 183 O VAL A 337 5518 5349 4487 -51 -1211 1125 O

ATOM 184 N ARG A 338 -10.744 28.747 -35.010 1.00 43.13 N

ANISOU 184 N ARG A 338 5988 5522 4876 -86 -1411 1285 N

ATOM 185 CA ARG A 338 -10.180 28.429 -36.313 1.00 42.71 C

ANISOU 185 CA ARG A 338 6063 5410 4754 -71 -1419 1230 C

ATOM 186 CB ARG A 338 -11.163 27.618 -37.158 1.00 46.74 C ANISOU 186 CB ARG A 338 6702 5799 5260 -108 -1550 1315 C ATOM 187 CG ARG A 338 -10.571 27.096 -38.459 1.00 60.82 C ANISOU 187 CG ARG A 338 8636 7511 6962 -96 -1564 1256 C ATOM 188 CD ARG A 338 -11.617 26.394 -39.315 1.00 71.08 C ANISOU 188 CD ARG A 338 10067 8693 8248 -157 -1692 1344 C ATOM 189 NE ARG A 338 -12.650 27.315 -39.775 1.00 77.04 N ANISOU 189 NE ARG A 338 10809 9425 9037 -239 -1716 1430 N ATOM 190 CZ ARG A 338 -12.594 27.989 -40.920 1.00 79.43 C ANISOU 190 CZ ARG A 338 11180 9697 9303 -282 -1689 1414 C ATOM 191 NH1 ARG A 338 -11.553 27.844 -41.729 1.00 70.85 N ANISOU 191 NH1 ARG A 338 10184 8593 8141 -252 -1638 1308 N ATOM 192 NH2 ARG A 338 -13.581 28.807 -41.255 1.00 80.11 N ANISOU 192 NH2 ARG A 338 11241 9769 9429 -352 -1710 1510 N ATOM 193 C ARG A 338 -9.798 29.711 -37.040 1.00 35.14 C ANISOU 193 C ARG A 338 5107 4468 3775 -102 -1318 1175 C ATOM 194 O ARG A 338 -8.771 29.761 -37.718 1.00 31.98 O ANISOU 194 O ARG A 338 4758 4081 3313 -72 -1261 1083 O ATOM 195 N LEU A 339 10.617 30.748 -36.883 1.00 26.23 N ANISOU 195 N LEU A 339 3924 3342 2703 -159 -1287 1235 N ATOM 196 CA LEU A 339 -10.405 32.001 -37.614 1.00 45.67 C ANISOU 196 CA LEU A 339 6393 5807 5152 -193 -1191 1198 C ATOM 197 CB LEU A 339 -11.714 32.792 -37.733 1.00 49.52 C ANISOU 197 CB LEU A 339 6859 6248 5708 -256 -1203 1315 C ATOM 198 CG LEU A 339 -12.793 32.146 -38.616 1.00 54.68 C ANISOU 198 CG LEU A 339 7610 6800 6367 -294 -1341 1427 C ATOM 199 CD1 LEU A 339 -14.150 32.824 -38.439 1.00 46.67 C ANISOU 199 CD1 LEU A 339 6541 5758 5434 -348 -1357 1568 C ATOM 200 CD2 LEU A 339 -12.375 32.136 -40.083 1.00 54.41 C ANISOU 200 CD2 LEU A 339 7700 6712 6259 -309 -1352 1381 C ATOM 201 C LEU A 339 -9.293 32.855 -36.998 1.00 44.54 C ANISOU 201 C LEU A 339 6159 5774 4989 -175 -1046 1090 C ATOM 202 O LEU A 339 -8.502 33.479 -37.715 1.00 33.96 O ANISOU 202 O LEU A 339 4851 4452 3602 -174 -965 1008 O ATOM 203 N TYR A 340 -9.226 32.881 -35.669 1.00 33.26 N ANISOU 203 N TYR A 340 4620 4424 3593 -167 -1014 1091 N ATOM 204 CA TYR A 340 -8.131 33.572 -35.006 1.00 26.38 C ANISOU 204 CA TYR A 340 3663 3669 2692 -162 -886 990 C ATOM 205 CB TYR A 340 -8.273 33.511 -33.488 1.00 26.13 C ANISOU 205 CB TYR A 340 3515 3716 2697 -169 -870 1012 C ATOM 206 CG TYR A 340 -9.362 34.386 -32.917 1.00 40.14 C ANISOU 206 CG TYR A 340 5238 5468 4546 -227 -831 1089 C ATOM 207 CD1 TYR A 340 -9.362 35.757 -33.132 1.00 37.85 C ANISOU 207 CD1 TYR A 340 4935 5184 4263 -275 -705 1063 C ATOM 208 CE1 TYR A 340 -10.352 36.563 -32.601 1.00 42.61 C ANISOU 208 CE1 TYR A 340 5494 5758 4937 -322 -653 1139 C ATOM 209 CD2 TYR A 340 -10.375 33.844 -32.134 1.00 40.37 C ANISOU 209 CD2 TYR A 340 5230 5468 4639 -231 -911 1189 C

ATOM 210 CE2 TYR A 340 -11.367 34.640 -31.599 1.00 51.12 C

ANISOU 210 CE2 TYR A 340 6544 6806 6072 -278 -865 1266 C

ATOM 211 CZ TYR A 340 -11.351 36.000 -31.835 1.00 48.75 C

ANISOU 211 CZ TYR A 340 6235 6507 5780 -321 -732 1243 C

ATOM 212 OH TYR A 340 -12.336 36.793 -31.298 1.00 43.74 O

ANISOU 212 OH TYR A 340 5558 5842 5221 -362 -672 1325 O

ATOM 213 C TYR A 340 -6.806 32.938 -35.419 1.00 29.60 C

ANISOU 213 C TYR A 340 4105 4120 3021 -103 -877 893 C

ATOM 214 O TYR A 340 -5.836 33.636 -35.698 1.00 29.32 O

ANISOU 214 O TYR A 340 4057 4146 2938 -105 -775 803 O

ATOM 215 N ARG A 341 -6.771 31.608 -35.450 1.00 23.38 N

ANISOU 215 N ARG A 341 3363 3299 2222 -50 -978 917 N

ATOM 216 CA ARG A 341 -5.554 30.898 -35.830 1.00 28.03 C

ANISOU 216 CA ARG A 341 3989 3919 2744 18 -965 841 C

ATOM 217 CB ARG A 341 -5.727 29.391 -35.666 1.00 35.54 C

ANISOU 217 CB ARG A 341 4986 4822 3697 75 -1074 888 C

ATOM 218 CG ARG A 341 -5.970 28.940 -34.232 1.00 36.74 C

ANISOU 218 CG ARG A 341 5026 5042 3892 88 -1104 934 C

ATOM 219 CD ARG A 341 -5.895 27.428 -34.135 1.00 41.74 C

ANISOU 219 CD ARG A 341 5709 5634 4518 157 -1192 966 C

ATOM 220 NE ARG A 341 -6.355 26.940 -32.840 1.00 43.24 N

ANISOU 220 NE ARG A 341 5804 5870 4755 163 -1240 1027 N

ATOM 221 CZ ARG A 341 -5.622 26.954 -31.734 1.00 38.82 C

ANISOU 221 CZ ARG A 341 5118 5442 4191 189 -1188 1002 C

ATOM 222 NH1 ARG A 341 -4.389 27.440 -31.757 1.00 31.75 N

ANISOU 222 NH1 ARG A 341 4169 4650 3243 208 -1087 920 N

ATOM 223 NH2 ARG A 341 -6.126 26.486 -30.600 1.00 39.56 N ANISOU 223 NH2 ARG A 341 5135 5569 4329 190 -1238 1063 N

ATOM 224 C ARG A 341 -5.154 31.216 -37.269 1.00 28.89 C

ANISOU 224 C ARG A 341 4210 3966 2803 17 -936 788 C

ATOM 225 0 ARG A 341 -3.972 31.369 -37.571 1.00 31.47 O

ANISOU 225 O ARG A 341 4534 4350 3074 52 -860 700 O

ATOM 226 N LYS A 342 -6.142 31.301 -38.153 1.00 26.05 N

ANISOU 226 N LYS A 342 3945 3492 2460 -26 -1000 848 N

ATOM 227 CA LYS A 342 -5.888 31.695 -39.537 1.00 43.79 C

ANISOU 227 CA LYS A 342 6300 5678 4661 -40 -975 806 C

ATOM 228 CB LYS A 342 -7.176 31.645 -40.359 1.00 53.77 C

ANISOU 228 CB LYS A 342 7658 6822 5949 -98 -1071 901 C

ATOM 229 CG LYS A 342 -6.964 31.812 -41.855 1.00 66.05 C

ANISOU 229 CG LYS A 342 9344 8305 7448 -117 -1068 867 C

ATOM 230 CD LYS A 342 -6.151 30.665 -42.430 1.00 74.23 C

ANISOU 230 CD LYS A 342 10488 9300 8416 -59 -1095 809 C

ATOM 231 CE LYS A 342 -6.001 30.799 -43.938 1.00 86.54 C

ANISOU 231 CE LYS A 342 12189 10777 9915 -86 -1094 777 C

ATOM 232 NZ LYS A 342 -5.248 29.658 -44.527 1.00 93.01 N ANISOU 232 NZ LYS A 342 13131 11543 10668 -31 -1110 723 N

ATOM 233 C LYS A 342 -5.271 33.095 -39.593 1.00 33.65 C

ANISOU 233 C LYS A 342 4954 4468 3365 -67 -841 734 C

ATOM 234 0 LYS A 342 -4.368 33.351 -40.390 1.00 29.68 O

ANISOU 234 O LYS A 342 4500 3974 2805 -49 -780 652 O

ATOM 235 N ALA A 343 -5.753 33.991 -38.735 1.00 32.81 N

ANISOU 235 N ALA A 343 4744 4412 3310 -112 -790 763 N

ATOM 236 CA ALA A 343 -5.204 35.347 -38.642 1.00 29.39 C ANISOU 236 CA ALA A 343 4251 4050 2866 -146 -651 695 C

ATOM 237 CB ALA A 343 -5.989 36.172 -37.638 1.00 23.08 C ANISOU 237 CB ALA A 343 3357 3280 2133 -199 -605 750 C

ATOM 238 C ALA A 343 -3.732 35.304 -38.249 1.00 28.92 C

ANISOU 238 C ALA A 343 4136 4108 2745 -107 -571 587 C

ATOM 239 O ALA A 343 -2.902 36.025 -38.802 1.00 22.85 O

ANISOU 239 O ALA A 343 3377 3375 1929 -113 -478 505 O

ATOM 240 N LEU A 344 -3.416 34.451 -37.281 1.00 36.78 N

ANISOU 240 N LEU A 344 5066 5168 3741 -67 -607 594 N

ATOM 241 CA LEU A 344 -2.041 34.298 -36.821 1.00 37.90 C

ANISOU 241 CA LEU A 344 5139 5436 3827 -28 -541 513 C

ATOM 242 CB LEU A 344 -1.996 33.433 -35.562 1.00 36.21 C

ANISOU 242 CB LEU A 344 4834 5293 3630 3 -590 551 C

ATOM 243 CG LEU A 344 -2.722 34.006 -34.347 1.00 34.49 C

ANISOU 243 CG LEU A 344 4519 5122 3465 -61 -572 594 C

ATOM 244 CD1 LEU A 344 -2.692 33.015 -33.198 1.00 34.57 C ANISOU 244 CD 1 LEU A 344 4450 5194 3490 -25 -633 637 C

ATOM 245 CD2 LEU A 344 -2.094 35.333 -33.944 1.00 29.89 C ANISOU 245 CD2 LEU A 344 3860 4646 2852 -127 -432 521 C

ATOM 246 C LEU A 344 -1.175 33.678 -37.912 1.00 27.69 C

ANISOU 246 C LEU A 344 3938 4110 2475 37 -548 462 C

ATOM 247 0 LEU A 344 -0.010 34.051 -38.086 1.00 28.60 O

ANISOU 247 O LEU A 344 4024 4309 2535 54 -460 381 O

ATOM 248 N GLU A 345 -1.747 32.723 -38.636 1.00 23.02 N

ANISOU 248 N GLU A 345 3460 3395 1892 70 -650 511 N

ATOM 249 CA GLU A 345 -1.037 32.072 -39.732 1.00 39.20 C ANISOU 249 CA GLU A 345 5620 5389 3886 129 -655 467 C

ATOM 250 CB GLU A 345 -1.918 31.000 -40.379 1.00 40.16 C

ANISOU 250 CB GLU A 345 5875 5365 4019 141 -777 535 C

ATOM 251 CG GLU A 345 -1.202 30.157 -41.418 1.00 45.01 C ANISOU 251 CG GLU A 345 6617 5911 4575 203 -779 493 C

ATOM 252 CD GLU A 345 -2.120 29.164 -42.100 1.00 58.88 C ANISOU 252 CD GLU A 345 8521 7518 6332 193 -894 556 C

ATOM 253 OE1 GLU A 345 -1.943 28.930 -43.314 1.00 70.83 O ANISOU 253 OE1 GLU A 345 10176 8940 7796 194 -897 527 O

ATOM 254 OE2 GLU A 345 -3.019 28.622 -41.427 1.00 54.30 O ANISOU 254 OE2 GLU A 345 7919 6913 5798 178 -981 635 O

ATOM 255 C GLU A 345 -0.614 33.106 -40.773 1.00 45.08 C ANISOU 255 C GLU A 345 6415 6121 4592 97 -573 399 C

ATOM 256 O GLU A 345 0.507 33.073 -41.279 1.00 46.31 O

ANISOU 256 O GLU A 345 6592 6313 4692 141 -510 326 O

ATOM 257 N VAL A 346 -1.523 34.027 -41.076 1.00 35.69 N

ANISOU 257 N VAL A 346 5243 4882 3436 23 -572 430 N

ATOM 258 CA VAL A 346 -1.278 35.092 -42.046 1.00 39.42 C

ANISOU 258 CA VAL A 346 5761 5337 3880 -14 -495 376 C

ATOM 259 CB VAL A 346 -2.596 35.786 -42.439 1.00 54.50 C

ANISOU 259 CB VAL A 346 7707 7161 5840 -86 -528 452 C ATOM 260 CGI VAL A 346 -2.318 37.135 -43.092 1.00 58.24 C ANISOU 260 CGI VAL A 346 8186 7646 6296 -130 -420 399 C ATOM 261 CG2 VAL A 346 -3.419 34.885 -43.352 1.00 55.95 C ANISOU 261 CG2 VAL A 346 8022 7212 6023 -87 -653 522 C

ATOM 262 C VAL A 346 -0.313 36.149 -41.514 1.00 39.71 C

ANISOU 262 C VAL A 346 5691 5505 3892 -31 -361 294 C

ATOM 263 O VAL A 346 0.565 36.621 -42.233 1.00 40.66 O

ANISOU 263 O VAL A 346 5841 5648 3961 -23 -285 216 O

ATOM 264 N PHE A 347 -0.479 36.509 -40.245 1.00 33.36 N

ANISOU 264 N PHE A 347 4766 4788 3121 -62 -331 311 N

ATOM 265 CA PHE A 347 0.306 37.572 -39.628 1.00 31.90 C

ANISOU 265 CA PHE A 347 4481 4730 2910 -102 -203 239 C

ATOM 266 C PHE A 347 0.601 37.215 -38.166 1.00 34.76 C

ANISOU 266 C PHE A 347 4716 5212 3278 -100 -201 249 C

ATOM 267 O PHE A 347 -0.150 37.569 -37.268 1.00 28.03 O

ANISOU 267 O PHE A 347 3805 4372 2473 -150 -199 295 O

ATOM 268 CB PHE A 347 -0.463 38.892 -39.740 1.00 46.61 C

ANISOU 268 CB PHE A 347 6345 6555 4809 -182 -136 253 C

ATOM 269 CG PHE A 347 0.207 40.059 -39.076 1.00 52.40 C

ANISOU 269 CG PHE A 347 6990 7404 5516 -241 4 181 C

ATOM 270 CD1 PHE A 347 1.570 40.250 -39.186 1.00 54.03 C

ANISOU 270 CD 1 PHE A 347 7165 7715 5647 -229 79 85 C

ATOM 271 CD2 PHE A 347 -0.540 40.986 -38.367 1.00 56.80 C

ANISOU 271 CD2 PHE A 347 7499 7962 6119 -313 66 212 C

ATOM 272 CE1 PHE A 347 2.182 41.332 -38.580 1.00 55.79 C

ANISOU 272 CE1 PHE A 347 7312 8048 5836 -298 207 19 C

ATOM 273 CE2 PHE A 347 0.061 42.071 -37.763 1.00 54.81 C ANISOU 273 CE2 PHE A 347 7182 7809 5835 -379 203 142 C

ATOM 274 CZ PHE A 347 1.426 42.245 -37.868 1.00 51.74 C

ANISOU 274 CZ PHE A 347 6764 7531 5366 -377 271 43 C

ATOM 275 N PRO A 348 1.705 36.493 -37.931 1.00 47.20 N

ANISOU 275 N PRO A 348 6250 6877 4805 -40 -199 213 N

ATOM 276 CD PRO A 348 2.624 36.062 -38.998 1.00 49.41 C

ANISOU 276 CD PRO A 348 6604 7138 5031 26 -189 162 C

ATOM 277 CA PRO A 348 2.062 35.908 -36.627 1.00 47.81 C

ANISOU 277 CA PRO A 348 6211 7072 4883 -24 -215 234 C

ATOM 278 CB PRO A 348 3.395 35.207 -36.914 1.00 53.53 C ANISOU 278 CB PRO A 348 6922 7870 5546 57 -198 192 C

ATOM 279 CG PRO A 348 3.350 34.906 -38.376 1.00 49.93 C

ANISOU 279 CG PRO A 348 6612 7281 5080 104 -224 178 C

ATOM 280 C PRO A 348 2.228 36.894 -35.463 1.00 44.52 C

ANISOU 280 C PRO A 348 5673 6784 4458 -111 -127 209 C

ATOM 281 O PRO A 348 1.977 36.512 -34.317 1.00 37.42 O

ANISOU 281 O PRO A 348 4691 5946 3582 -122 -160 252 O

ATOM 282 N GLU A 349 2.651 38.124 -35.742 1.00 42.10 N

ANISOU 282 N GLU A 349 4970 6931 4094 222 325 17 N

ATOM 283 CA GLU A 349 2.866 39.115 -34.687 1.00 43.23 C

ANISOU 283 CA GLU A 349 5147 6967 4312 236 356 88 C

ATOM 284 CB GLU A 349 4.110 39.952 -34.992 1.00 41.50 C

ANISOU 284 CB GLU A 349 4929 6738 4100 242 414 112 C

ATOM 285 CG GLU A 349 5.385 39.140 -35.158 1.00 32.46 C

ANISOU 285 CG GLU A 349 3781 5579 2974 223 414 5 C

ATOM 286 CD GLU A 349 5.881 38.558 -33.852 1.00 45.09 C

ANISOU 286 CD GLU A 349 5411 7050 4673 211 389 -61 C ATOM 287 OE1 GLU A 349 6.267 39.340 -32.960 1.00 48.50 O

ANISOU 287 OE1 GLU A 349 5869 7388 5170 221 414 -18 O ATOM 288 OE2 GLU A 349 5.892 37.319 -33.715 1.00 53.07 O

ANISOU 288 OE2 GLU A 349 6417 8053 5696 193 345 -156 O

ATOM 289 C GLU A 349 1.649 40.027 -34.494 1.00 34.56 C

ANISOU 289 C GLU A 349 4052 5878 3204 255 361 200 C

ATOM 290 O GLU A 349 1.773 41.250 -34.462 1.00 34.38 O

ANISOU 290 O GLU A 349 4034 5840 3189 273 406 292 O

ATOM 291 N PHE A 350 0.474 39.422 -34.364 1.00 37.61 N

ANISOU 291 N PHE A 350 4431 6284 3576 252 315 192 N

ATOM 292 CA PHE A 350 -0.774 40.172 -34.254 1.00 33.26 C

ANISOU 292 CA PHE A 350 3877 5747 3012 270 315 292 C

ATOM 293 CB PHE A 350 -1.828 39.545 -35.170 1.00 40.88 C

ANISOU 293 CB PHE A 350 4808 6825 3901 267 274 280 C

ATOM 294 CG PHE A 350 -3.055 40.396 -35.383 1.00 37.16 C

ANISOU 294 CG PHE A 350 4324 6395 3400 287 278 390 C

ATOM 295 CD1 PHE A 350 -3.241 41.572 -34.675 1.00 41.93 C

ANISOU 295 CD 1 PHE A 350 4949 6929 4054 305 314 487 C

ATOM 296 CD2 PHE A 350 -4.024 40.009 -36.297 1.00 33.36 C

ANISOU 296 CD2 PHE A 350 3809 6024 2844 288 243 392 C

ATOM 297 CE1 PHE A 350 -4.370 42.347 -34.873 1.00 39.64 C

ANISOU 297 CE1 PHE A 350 4644 6675 3743 323 317 588 C

ATOM 298 CE2 PHE A 350 -5.156 40.782 -36.503 1.00 28.60 C

ANISOU 298 CE2 PHE A 350 3192 5460 2216 307 244 494 C

ATOM 299 CZ PHE A 350 -5.330 41.951 -35.790 1.00 31.06 C

ANISOU 299 CZ PHE A 350 3522 5697 2580 324 281 593 C

ATOM 300 C PHE A 350 -1.248 40.159 -32.800 1.00 38.65 C

ANISOU 300 C PHE A 350 4593 6310 3782 270 300 301 C

ATOM 301 O PHE A 350 -1.929 39.230 -32.376 1.00 26.69 O ANISOU 301 O PHE A 350 3080 4778 2284 260 255 253 O

ATOM 302 N ALA A 351 -0.874 41.189 -32.043 1.00 21.32 N

ANISOU 302 N ALA A 351 2423 4033 1643 283 340 362 N

ATOM 303 CA ALA A 351 -1.170 41.258 -30.614 1.00 27.02 C

ANISOU 303 CA ALA A 351 3180 4639 2446 285 332 368 C

ATOM 304 CB ALA A 351 -0.659 42.569 -30.028 1.00 29.42 C

ANISOU 304 CB ALA A 351 3504 4873 2801 301 383 439 C

ATOM 305 C ALA A 351 -2.651 41.068 -30.283 1.00 29.55 C

ANISOU 305 C ALA A 351 3497 4965 2766 289 300 403 C

ATOM 306 O ALA A 351 -2.987 40.369 -29.331 1.00 29.08 O

ANISOU 306 O ALA A 351 3457 4837 2753 280 270 361 O

ATOM 307 N ALA A 352 -3.530 41.689 -31.062 1.00 29.09 N

ANISOU 307 N ALA A 352 3413 4986 2655 303 308 482 N

ATOM 308 CA ALA A 352 -4.966 41.624 -30.784 1.00 30.95 C

ANISOU 308 CA ALA A 352 3641 5226 2892 308 282 523 C

ATOM 309 CB ALA A 352 -5.718 42.679 -31.593 1.00 45.61 C

ANISOU 309 CB ALA A 352 5470 7158 4701 328 305 631 C

ATOM 310 C ALA A 352 -5.546 40.233 -31.042 1.00 31.39 C

ANISOU 310 C ALA A 352 3680 5324 2923 291 225 442 C

ATOM 311 O ALA A 352 -6.434 39.778 -30.315 1.00 29.47 O

ANISOU 311 O ALA A 352 3444 5037 2717 288 198 436 O

ATOM 312 N ALA A 353 -5.048 39.554 -32.071 1.00 29.52 N

ANISOU 312 N ALA A 353 3418 5171 2628 279 210 378 N

ATOM 313 CA ALA A 353 -5.532 38.209 -32.372 1.00 36.30 C

ANISOU 313 CA ALA A 353 4255 6070 3468 262 156 293 C

ATOM 314 CB ALA A 353 -4.976 37.710 -33.698 1.00 32.99 C

ANISOU 314 CB ALA A 353 3803 5761 2970 253 148 235 C

ATOM 315 C ALA A 353 -5.140 37.268 -31.240 1.00 33.39 C

ANISOU 315 C ALA A 353 3913 5596 3176 245 134 212 C

ATOM 316 O ALA A 353 -5.924 36.414 -30.819 1.00 25.37 O

ANISOU 316 O ALA A 353 2893 4559 2187 236 95 177 O

ATOM 317 N HIS A 354 -3.921 37.436 -30.743 1.00 25.98 N

ANISOU 317 N HIS A 354 3004 4592 2277 242 160 186 N

ATOM 318 CA HIS A 354 -3.447 36.622 -29.638 1.00 21.84 C

ANISOU 318 CA HIS A 354 2507 3966 1826 229 141 117 C

ATOM 319 CB HIS A 354 -1.960 36.864 -29.375 1.00 26.46 C

ANISOU 319 CB HIS A 354 3113 4500 2439 226 170 86 C

ATOM 320 CG HIS A 354 -1.052 36.054 -30.251 1.00 24.98 C

ANISOU 320 CG HIS A 354 2903 4366 2221 209 159 -4 C

ATOM 321 CD2 HIS A 354 -0.146 36.428 -31.187 1.00 23.65 C

ANISOU 321 CD2 HIS A 354 2720 4258 2009 210 189 -11 C

ATOM 322 ND1 HIS A 354 -1.002 34.677 -30.201 1.00 19.58 N

ANISOU 322 ND1 HIS A 354 2207 3676 1556 189 116 -102 N

ATOM 323 CE1 HIS A 354 -0.106 34.237 -31.068 1.00 23.91 C

ANISOU 323 CE1 HIS A 354 2734 4277 2073 178 119 -170 C

ATOM 324 NE2 HIS A 354 0.426 35.280 -31.681 1.00 25.71 N ANISOU 324 NE2 HIS A 354 2960 4548 2260 190 163 -116 N

ATOM 325 C HIS A 354 -4.267 36.890 -28.380 1.00 29.10 C

ANISOU 325 C HIS A 354 3454 4798 2804 237 139 167 C

ATOM 326 O HIS A 354 -4.706 35.960 -27.712 1.00 24.87 O

ANISOU 326 O HIS A 354 2924 4216 2308 227 105 122 O

ATOM 327 N SER A 355 -4.476 38.162 -28.065 1.00 21.31 N

ANISOU 327 N SER A 355 2483 3788 1825 256 177 259 N

ATOM 328 CA SER A 355 -5.221 38.519 -26.865 1.00 24.90 C

ANISOU 328 CA SER A 355 2965 4160 2335 265 181 307 C

ATOM 329 CB SER A 355 -5.131 40.026 -26.601 1.00 27.29 C

ANISOU 329 CB SER A 355 3283 4436 2650 286 231 400 C

ATOM 330 OG SER A 355 -5.949 40.395 -25.503 1.00 53.46 O

ANISOU 330 OG SER A 355 6621 7679 6014 295 236 447 O

ATOM 331 C SER A 355 -6.675 38.048 -26.953 1.00 30.85 C

ANISOU 331 C SER A 355 3698 4946 3078 264 149 325 C

ATOM 332 O SER A 355 -7.266 37.652 -25.947 1.00 26.95 O

ANISOU 332 O SER A 355 3223 4384 2633 262 134 321 O

ATOM 333 N ASN A 356 -7.243 38.072 -28.157 1.00 28.31 N

ANISOU 333 N ASN A 356 3337 4730 2691 266 138 343 N

ATOM 334 CA ASN A 356 -8.605 37.590 -28.373 1.00 28.08 C

ANISOU 334 CA ASN A 356 3280 4739 2648 265 104 353 C

ATOM 335 CB ASN A 356 -9.120 38.010 -29.754 1.00 44.26 C

ANISOU 335 CB ASN A 356 5287 6911 4618 274 102 395 C

ATOM 336 CG ASN A 356 -9.584 39.450 -29.795 1.00 42.50 C

ANISOU 336 CG ASN A 356 5066 6695 4387 297 141 512 C

ATOM 337 OD1 ASN A 356 -9.943 40.025 -28.770 1.00 33.41 O

ANISOU 337 OD1 ASN A 356 3940 5460 3292 306 161 562 O

ATOM 338 ND2 ASN A 356 -9.588 40.037 -30.988 1.00 40.81 N

ANISOU 338 ND2 ASN A 356 4823 6582 4102 307 152 557 N

ATOM 339 C ASN A 356 -8.712 36.077 -28.248 1.00 29.32 C

ANISOU 339 C ASN A 356 3427 4888 2825 244 57 254 C

ATOM 340 O ASN A 356 -9.613 35.556 -27.595 1.00 28.31 O

ANISOU 340 O ASN A 356 3299 4719 2737 241 34 252 O

ATOM 341 N LEU A 357 -7.806 35.370 -28.907 1.00 21.50 N

ANISOU 341 N LEU A 357 2423 3938 1810 230 43 173 N

ATOM 342 CA LEU A 357 -7.792 33.915 -28.831 1.00 31.06 C

ANISOU 342 CA LEU A 357 3618 5137 3045 209 -1 74 C

ATOM 343 CB LEU A 357 -6.715 33.340 -29.757 1.00 28.73 C

ANISOU 343 CB LEU A 357 3304 4900 2713 196 -8 -10 C

ATOM 344 CG LEU A 357 -6.536 31.822 -29.801 1.00 31.68 C

ANISOU 344 CG LEU A 357 3657 5266 3115 173 -51 -123 C

ATOM 345 CD1 LEU A 357 -7.859 31.112 -30.077 1.00 29.33 C

ANISOU 345 CD 1 LEU A 357 3323 5007 2814 168 -92 -137 C

ATOM 346 CD2 LEU A 357 -5.503 31.456 -30.853 1.00 38.80 C

ANISOU 346 CD2 LEU A 357 4535 6237 3969 162 -50 -197 C

ATOM 347 C LEU A 357 -7.559 33.477 -27.386 1.00 25.39 C ANISOU 347 C LEU A 357 2939 4296 2412 204 -3 52 C

ATOM 348 0 LEU A 357 -8.142 32.497 -26.922 1.00 23.74 O

ANISOU 348 O LEU A 357 2722 4052 2244 194 -36 12 O

ATOM 349 N ALA A 358 -6.716 34.214 -26.667 1.00 24.47 N

ANISOU 349 N ALA A 358 2863 4113 2322 212 31 81 N

ATOM 350 CA ALA A 358 -6.448 33.893 -25.261 1.00 25.87 C

ANISOU 350 CA ALA A 358 3080 4177 2573 210 30 66 C

ATOM 351 CB ALA A 358 -5.349 34.789 -24.702 1.00 21.40 C

ANISOU 351 CB ALA A 358 2551 3554 2024 219 68 90 C

ATOM 352 C ALA A 358 -7.706 33.997 -24.400 1.00 26.44 C

ANISOU 352 C ALA A 358 3163 4203 2679 218 27 122 C

ATOM 353 O ALA A 358 -8.009 33.102 -23.599 1.00 19.89 O

ANISOU 353 O ALA A 358 2342 3315 1900 209 3 88 O

ATOM 354 N SER A 359 -8.432 35.096 -24.562 1.00 27.72 N

ANISOU 354 N SER A 359 3323 4392 2818 235 52 209 N

ATOM 355 CA SER A 359 -9.675 35.310 -23.831 1.00 33.44 C

ANISOU 355 CA SER A 359 4054 5079 3572 243 54 267 C

ATOM 356 CB SER A 359 -10.288 36.657 -24.229 1.00 44.67 C

ANISOU 356 CB SER A 359 5468 6540 4962 263 86 363 C

ATOM 357 OG SER A 359 -11.570 36.834 -23.652 1.00 49.39 O

ANISOU 357 OG SER A 359 6066 7112 5588 271 87 417 O

ATOM 358 C SER A 359 -10.659 34.163 -24.096 1.00 35.23 C

ANISOU 358 C SER A 359 4247 5333 3805 231 11 227 C

ATOM 359 0 SER A 359 -11.264 33.618 -23.169 1.00 27.12 O

ANISOU 359 O SER A 359 3232 4243 2830 228 -1 224 O

ATOM 360 N VAL A 360 -10.794 33.794 -25.367 1.00 25.88 N

ANISOU 360 N VAL A 360 3019 4245 2569 224 -12 195 N

ATOM 361 CA VAL A 360 -11.696 32.729 -25.794 1.00 27.58 C

ANISOU 361 CA VAL A 360 3194 4498 2788 213 -55 151 C

ATOM 362 CB VAL A 360 -11.683 32.576 -27.330 1.00 46.15 C

ANISOU 362 CB VAL A 360 5498 6970 5065 208 -75 120 C

ATOM 363 CGI VAL A 360 -12.283 31.245 -27.741 1.00 50.26 C ANISOU 363 CGI VAL A 360 5976 7522 5598 191 -125 42 C

ATOM 364 CG2 VAL A 360 -12.415 33.733 -27.990 1.00 51.21 C

ANISOU 364 CG2 VAL A 360 6123 7681 5653 227 -57 211 C

ATOM 365 C VAL A 360 -11.314 31.395 -25.172 1.00 34.33 C

ANISOU 365 C VAL A 360 4054 5291 3701 194 -83 65 C

ATOM 366 O VAL A 360 -12.154 30.690 -24.609 1.00 29.38 O

ANISOU 366 O VAL A 360 3418 4623 3121 189 -104 57 O

ATOM 367 N LEU A 361 -10.039 31.047 -25.278 1.00 21.20 N

ANISOU 367 N LEU A 361 2401 3618 2037 184 -83 3 N

ATOM 368 CA LEU A 361 -9.541 29.821 -24.673 1.00 24.37 C

ANISOU 368 CA LEU A 361 2807 3956 2498 168 -108 -76 C

ATOM 369 CB LEU A 361 -8.045 29.631 -24.985 1.00 27.96 C

ANISOU 369 CB LEU A 361 3270 4412 2942 159 -104 -139 C

ATOM 370 CG LEU A 361 -7.669 29.325 -26.444 1.00 35.44 C ANISOU 370 CG LEU A 361 4173 5463 3829 149 -118 -198 C

ATOM 371 CD1 LEU A 361 -6.161 29.472 -26.701 1.00 18.99 C

ANISOU 371 CD 1 LEU A 361 2104 3380 1733 145 -100 -240 C

ATOM 372 CD2 LEU A 361 -8.155 27.936 -26.860 1.00 28.76 C

ANISOU 372 CD2 LEU A 361 3282 4641 3006 131 -164 -281 C

ATOM 373 C LEU A 361 -9.794 29.847 -23.166 1.00 22.13 C

ANISOU 373 C LEU A 361 2565 3563 2279 174 -97 -37 C

ATOM 374 0 LEU A 361 -10.231 28.850 -22.587 1.00 27.69 O

ANISOU 374 O LEU A 361 3263 4219 3038 164 -121 -69 O

ATOM 375 N GLN A 362 -9.541 30.994 -22.539 1.00 19.37 N

ANISOU 375 N GLN A 362 2257 3177 1924 190 -59 31 N

ATOM 376 CA GLN A 362 -9.760 31.137 -21.103 1.00 21.60 C

ANISOU 376 CA GLN A 362 2583 3364 2261 198 -44 70 C

ATOM 377 CB GLN A 362 -9.388 32.538 -20.601 1.00 22.82 C

ANISOU 377 CB GLN A 362 2777 3491 2402 216 -0 139 C

ATOM 378 CG GLN A 362 -9.464 32.636 -19.073 1.00 27.76 C

ANISOU 378 CG GLN A 362 3449 4018 3079 224 14 167 C

ATOM 379 CD GLN A 362 -9.436 34.060 -18.542 1.00 51.90 C

ANISOU 379 CD GLN A 362 6540 7050 6129 243 58 240 C

ATOM 380 OE1 GLN A 362 -10.009 34.344 -17.489 1.00 57.71 O

ANISOU 380 OE1 GLN A 362 7304 7729 6895 253 74 283 O

ATOM 381 NE2 GLN A 362 -8.766 34.960 -19.263 1.00 42.53 N

ANISOU 381 NE2 GLN A 362 5350 5905 4905 249 80 255 N

ATOM 382 C GLN A 362 -11.209 30.849 -20.736 1.00 26.73 C

ANISOU 382 C GLN A 362 3218 4001 2937 200 -53 105 C

ATOM 383 O GLN A 362 -11.477 30.224 -19.712 1.00 24.02 O

ANISOU 383 O GLN A 362 2893 3586 2648 197 -60 100 O

ATOM 384 N GLN A 363 -12.141 31.312 -21.565 1.00 36.86 N

ANISOU 384 N GLN A 363 4469 5355 4182 206 -53 145 N

ATOM 385 CA GLN A 363 -13.561 31.095 -21.296 1.00 41.10 C

ANISOU 385 CA GLN A 363 4987 5884 4745 209 -61 180 C

ATOM 386 CB GLN A 363 -14.437 32.021 -22.143 1.00 46.30 C

ANISOU 386 CB GLN A 363 5619 6618 5356 221 -51 244 C

ATOM 387 CG GLN A 363 -14.313 33.488 -21.771 1.00 58.94 C

ANISOU 387 CG GLN A 363 7252 8201 6940 240 -5 327 C

ATOM 388 CD GLN A 363 -15.312 34.367 -22.498 1.00 72.21 C

ANISOU 388 CD GLN A 363 8904 9947 8585 254 4 398 C

ATOM 389 OE1 GLN A 363 -15.112 35.575 -22.626 1.00 76.99 O

ANISOU 389 OE1 GLN A 363 9522 10564 9165 268 38 460 O

ATOM 390 NE2 GLN A 363 -16.393 33.764 -22.979 1.00 74.72 N

ANISOU 390 NE2 GLN A 363 9180 10305 8905 248 -26 390 N

ATOM 391 C GLN A 363 -13.950 29.641 -21.521 1.00 38.49 C

ANISOU 391 C GLN A 363 4618 5557 4448 190 -104 109 C

ATOM 392 O GLN A 363 -14.901 29.150 -20.923 1.00 31.36 O

ANISOU 392 O GLN A 363 3709 4614 3594 189 -112 123 O

ATOM 393 N GLN A 364 -13.210 28.953 -22.382 1.00 31.95 N ANISOU 393 N GLN A 364 3763 4775 3600 176 -130 31 N

ATOM 394 CA GLN A 364 -13.460 27.537 -22.630 1.00 35.08 C

ANISOU 394 CA GLN A 364 4120 5174 4036 158 -171 -48 C

ATOM 395 CB GLN A 364 -12.890 27.112 -23.985 1.00 36.66 C

ANISOU 395 CB GLN A 364 4278 5462 4188 145 -197 -123 C

ATOM 396 CG GLN A 364 -13.635 27.663 -25.187 1.00 50.55 C

ANISOU 396 CG GLN A 364 5998 7328 5879 152 -203 -98 C

ATOM 397 CD GLN A 364 -13.144 27.066 -26.493 1.00 51.95 C

ANISOU 397 CD GLN A 364 6132 7596 6011 139 -232 -183 C

ATOM 398 OE1 GLN A 364 -11.941 26.999 -26.741 1.00 42.42 O

ANISOU 398 OE1 GLN A 364 4937 6395 4785 132 -225 -228 O

ATOM 399 NE2 GLN A 364 -14.075 26.625 -27.333 1.00 57.56 N

ANISOU 399 NE2 GLN A 364 6790 8377 6704 134 -264 -208 N

ATOM 400 C GLN A 364 -12.859 26.675 -21.527 1.00 32.37 C

ANISOU 400 C GLN A 364 3803 4733 3762 149 -176 -85 C

ATOM 401 O GLN A 364 -13.051 25.458 -21.501 1.00 36.79 O

ANISOU 401 O GLN A 364 4333 5273 4372 134 -207 -145 O

ATOM 402 N GLY A 365 -12.119 27.308 -20.621 1.00 24.16 N

ANISOU 402 N GLY A 365 2818 3634 2729 159 -147 -50 N

ATOM 403 CA GLY A 365 -11.454 26.597 -19.545 1.00 26.22 C

ANISOU 403 CA GLY A 365 3108 3806 3048 153 -152 -79 C

ATOM 404 C GLY A 365 -10.125 25.999 -19.985 1.00 27.52 C

ANISOU 404 C GLY A 365 3266 3977 3214 139 -169 -161 C

ATOM 405 O GLY A 365 -9.555 25.149 -19.299 1.00 30.76 O

ANISOU 405 O GLY A 365 3687 4321 3677 131 -183 -201 O

ATOM 406 N LYS A 366 -9.638 26.444 -21.137 1.00 24.55 N

ANISOU 406 N LYS A 366 2870 3680 2776 138 -168 -183 N

ATOM 407 CA LYS A 366 -8.348 26.009 -21.658 1.00 19.12 C

ANISOU 407 CA LYS A 366 2174 3007 2082 126 -179 -260 C

ATOM 408 CB LYS A 366 -8.404 25.873 -23.184 1.00 24.77 C

ANISOU 408 CB LYS A 366 2840 3830 2743 117 -194 -307 C

ATOM 409 CG LYS A 366 -9.405 24.816 -23.649 1.00 29.99 C

ANISOU 409 CG LYS A 366 3447 4519 3429 104 -230 -351 C

ATOM 410 CD LYS A 366 -9.497 24.723 -25.163 1.00 31.01 C

ANISOU 410 CD LYS A 366 3526 4762 3495 97 -246 -399 C

ATOM 411 CE LYS A 366 -10.573 23.729 -25.576 1.00 42.82 C

ANISOU 411 CE LYS A 366 4967 6283 5019 86 -284 -443 C

ATOM 412 NZ LYS A 366 -10.600 23.505 -27.045 1.00 48.14 N

ANISOU 412 NZ LYS A 366 5588 7070 5632 78 -305 -504 N

ATOM 413 C LYS A 366 -7.268 26.998 -21.229 1.00 27.69 C

ANISOU 413 C LYS A 366 3309 4065 3147 137 -147 -229 C

ATOM 414 0 LYS A 366 -6.762 27.781 -22.028 1.00 22.13 O

ANISOU 414 O LYS A 366 2603 3420 2387 142 -129 -222 O

ATOM 415 N LEU A 367 -6.917 26.938 -19.950 1.00 20.50 N

ANISOU 415 N LEU A 367 2440 3063 2284 142 -140 -211 N

ATOM 416 CA LEU A 367 -6.087 27.958 -19.327 1.00 22.15 C ANISOU 416 CA LEU A 367 2699 3236 2482 156 -109 -172 C

ATOM 417 CB LEU A 367 -6.182 27.843 -17.811 1.00 19.81 C

ANISOU 417 CB LEU A 367 2446 2844 2236 163 -105 -140 C

ATOM 418 CG LEU A 367 -7.612 27.757 -17.268 1.00 16.59 C

ANISOU 418 CG LEU A 367 2037 2420 1846 169 -103 -86 C

ATOM 419 CD1 LEU A 367 -7.587 27.663 -15.748 1.00 23.09 C

ANISOU 419 CD 1 LEU A 367 2907 3153 2714 178 -96 -56 C

ATOM 420 CD2 LEU A 367 -8.440 28.944 -17.727 1.00 16.90 C

ANISOU 420 CD2 LEU A 367 2074 2512 1837 183 -75 -17 C

ATOM 421 C LEU A 367 -4.628 27.905 -19.762 1.00 22.93 C

ANISOU 421 C LEU A 367 2798 3341 2572 148 -110 -231 C

ATOM 422 0 LEU A 367 -4.032 28.935 -20.053 1.00 18.40 O

ANISOU 422 O LEU A 367 2240 2790 1961 158 -82 -206 O

ATOM 423 N GLN A 368 -4.042 26.712 -19.780 1.00 18.73 N

ANISOU 423 N GLN A 368 2248 2785 2083 132 -140 -309 N

ATOM 424 CA GLN A 368 -2.659 26.579 -20.233 1.00 22.51 C

ANISOU 424 CA GLN A 368 2723 3270 2560 124 -142 -371 C

ATOM 425 CB GLN A 368 -2.199 25.126 -20.157 1.00 15.00 C

ANISOU 425 CB GLN A 368 1747 2284 1669 105 -179 -456 C

ATOM 426 CG GLN A 368 -1.917 24.650 -18.757 1.00 19.36 C

ANISOU 426 CG GLN A 368 2333 2734 2287 108 -191 -448 C

ATOM 427 CD GLN A 368 -1.554 23.181 -18.732 1.00 35.91 C

ANISOU 427 CD GLN A 368 4398 4796 4449 89 -227 -527 C

ATOM 428 OE1 GLN A 368 -0.494 22.803 -18.249 1.00 46.31 O

ANISOU 428 OE1 GLN A 368 5729 6059 5807 86 -238 -563 O

ATOM 429 NE2 GLN A 368 -2.434 22.346 -19.270 1.00 36.23 N

ANISOU 429 NE2 GLN A 368 4394 4867 4504 78 -248 -556 N

ATOM 430 C GLN A 368 -2.487 27.094 -21.656 1.00 19.28 C

ANISOU 430 C GLN A 368 2283 2960 2084 121 -129 -385 C

ATOM 431 O GLN A 368 -1.480 27.734 -21.986 1.00 18.54 O

ANISOU 431 O GLN A 368 2200 2879 1964 124 -107 -392 O

ATOM 432 N GLU A 369 -3.466 26.807 -22.500 1.00 22.00 N

ANISOU 432 N GLU A 369 2587 3373 2397 116 -141 -390 N

ATOM 433 CA GLU A 369 -3.411 27.248 -23.885 1.00 22.34 C

ANISOU 433 CA GLU A 369 2599 3521 2370 115 -131 -400 C

ATOM 434 CB GLU A 369 -4.473 26.532 -24.727 1.00 21.25 C

ANISOU 434 CB GLU A 369 2410 3452 2214 106 -159 -429 C

ATOM 435 CG GLU A 369 -4.101 26.478 -26.184 1.00 23.51 C

ANISOU 435 CG GLU A 369 2655 3841 2436 98 -162 -481 C

ATOM 436 CD GLU A 369 -5.039 25.633 -27.008 1.00 34.29 C

ANISOU 436 CD GLU A 369 3966 5273 3788 86 -196 -528 C

ATOM 437 OE1 GLU A 369 -5.884 24.913 -26.426 1.00 24.77 O

ANISOU 437 OE1 GLU A 369 2751 4024 2637 82 -220 -532 O

ATOM 438 OE2 GLU A 369 -4.913 25.691 -28.245 1.00 27.16 O

ANISOU 438 OE2 GLU A 369 3030 4469 2821 82 -197 -561 O

ATOM 439 C GLU A 369 -3.571 28.763 -23.985 1.00 21.20 C ANISOU 439 C GLU A 369 2479 3405 2172 135 -91 -310 C

ATOM 440 O GLU A 369 -2.867 29.419 -24.752 1.00 23.16 O

ANISOU 440 O GLU A 369 2723 3704 2373 138 -68 -309 O

ATOM 441 N ALA A 370 -4.499 29.315 -23.209 1.00 18.40 N

ANISOU 441 N ALA A 370 2148 3015 1828 149 -80 -234 N

ATOM 442 CA ALA A 370 -4.709 30.763 -23.170 1.00 18.30 C

ANISOU 442 CA ALA A 370 2159 3018 1778 168 -41 -145 C

ATOM 443 CB ALA A 370 -5.842 31.102 -22.203 1.00 25.88 C

ANISOU 443 CB ALA A 370 3140 3930 2764 180 -35 -74 C

ATOM 444 C ALA A 370 -3.416 31.486 -22.767 1.00 17.54 C

ANISOU 444 C ALA A 370 2097 2878 1690 175 -12 -140 C

ATOM 445 O ALA A 370 -3.054 32.516 -23.330 1.00 19.90 O

ANISOU 445 O ALA A 370 2397 3217 1948 185 20 -102 O

ATOM 446 N LEU A 371 -2.716 30.921 -21.792 1.00 16.34 N

ANISOU 446 N LEU A 371 1972 2643 1595 170 -24 -179 N

ATOM 447 CA LEU A 371 -1.443 31.469 -21.324 1.00 18.69 C

ANISOU 447 CA LEU A 371 2300 2891 1910 175 -4 -185 C

ATOM 448 CB LEU A 371 -0.855 30.548 -20.261 1.00 19.40 C

ANISOU 448 CB LEU A 371 2412 2894 2065 167 -30 -235 C

ATOM 449 CG LEU A 371 -0.369 31.194 -18.975 1.00 31.30 C

ANISOU 449 CG LEU A 371 3970 4317 3606 181 -14 -201 C

ATOM 450 CD1 LEU A 371 -1.517 31.957 -18.299 1.00 29.02 C

ANISOU 450 CD 1 LEU A 371 3704 4014 3310 197 5 -117 C

ATOM 451 CD2 LEU A 371 0.219 30.126 -18.062 1.00 12.89 C

ANISOU 451 CD2 LEU A 371 1653 1910 1334 172 -47 -255 C

ATOM 452 C LEU A 371 -0.411 31.679 -22.437 1.00 25.35 C

ANISOU 452 C LEU A 371 3122 3792 2718 169 9 -224 C

ATOM 453 0 LEU A 371 0.287 32.700 -22.461 1.00 17.57 O

ANISOU 453 O LEU A 371 2153 2801 1722 179 43 -193 O

ATOM 454 N MET A 372 -0.296 30.703 -23.338 1.00 17.73 N

ANISOU 454 N MET A 372 2118 2880 1740 152 -16 -295 N

ATOM 455 CA MET A 372 0.615 30.818 -24.481 1.00 14.92 C

ANISOU 455 CA MET A 372 1736 2588 1345 145 -2 -337 C

ATOM 456 CB MET A 372 0.423 29.654 -25.453 1.00 21.15 C

ANISOU 456 CB MET A 372 2477 3441 2116 126 -34 -415 C

ATOM 457 CG MET A 372 1.109 28.370 -25.059 1.00 23.92 C

ANISOU 457 CG MET A 372 2821 3736 2531 109 -66 -506 C

ATOM 458 SD MET A 372 0.912 27.100 -26.331 1.00 29.20 S

ANISOU 458 SD MET A 372 3427 4488 3178 87 -99 -604 S

ATOM 459 CE MET A 372 1.625 27.918 -27.758 1.00 87.52 C

ANISOU 459 CE MET A 372 10794 11980 10479 89 -62 -608 C

ATOM 460 C MET A 372 0.368 32.102 -25.248 1.00 21.94 C

ANISOU 460 C MET A 372 2620 3546 2168 160 37 -264 C

ATOM 461 O MET A 372 1.308 32.789 -25.655 1.00 24.04 O

ANISOU 461 O MET A 372 2889 3827 2417 164 68 -259 O

ATOM 462 N HIS A 373 -0.905 32.406 -25.471 1.00 23.10 N ANISOU 462 N HIS A 373 2756 3737 2283 168 35 -206 N

ATOM 463 CA HIS A 373 -1.269 33.554 -26.286 1.00 18.55 C

ANISOU 463 CA HIS A 373 2169 3235 1644 183 68 -133 C

ATOM 464 CB HIS A 373 -2.650 33.344 -26.907 1.00 20.97 C

ANISOU 464 CB HIS A 373 2444 3614 1908 184 48 -107 C

ATOM 465 CG HIS A 373 -2.684 32.199 -27.871 1.00 28.15 C

ANISOU 465 CG HIS A 373 3311 4594 2790 166 14 -192 C

ATOM 466 CD2 HIS A 373 -3.036 30.901 -27.705 1.00 24.57 C

ANISOU 466 CD2 HIS A 373 2840 4126 2371 149 -28 -263 C

ATOM 467 ND1 HIS A 373 -2.265 32.318 -29.179 1.00 26.44 N

ANISOU 467 ND1 HIS A 373 3063 4476 2506 163 24 -214 N

ATOM 468 CE1 HIS A 373 -2.381 31.150 -29.784 1.00 27.50 C

ANISOU 468 CE1 HIS A 373 3162 4655 2630 145 -13 -300 C

ATOM 469 NE2 HIS A 373 -2.845 30.273 -28.912 1.00 24.71 N

ANISOU 469 NE2 HIS A 373 2815 4232 2342 137 -45 -331 N

ATOM 470 C HIS A 373 -1.160 34.852 -25.510 1.00 21.06 C

ANISOU 470 C HIS A 373 2524 3497 1982 202 107 -51 C

ATOM 471 O HIS A 373 -0.776 35.873 -26.064 1.00 16.81 O

ANISOU 471 O HIS A 373 1982 2994 1411 213 144 -5 O

ATOM 472 N TYR A 374 -1.460 34.819 -24.215 1.00 14.24 N

ANISOU 472 N TYR A 374 1694 2544 1173 206 101 -33 N

ATOM 473 CA TYR A 374 -1.231 36.012 -23.419 1.00 13.79 C

ANISOU 473 CA TYR A 374 1670 2428 1140 223 137 32 C

ATOM 474 CB TYR A 374 -1.715 35.825 -21.979 1.00 15.76 C

ANISOU 474 CB TYR A 374 1956 2587 1444 228 125 46 C

ATOM 475 CG TYR A 374 -3.209 35.969 -21.821 1.00 20.33 C

ANISOU 475 CG TYR A 374 2530 3183 2013 235 121 105 C

ATOM 476 CD1 TYR A 374 -3.866 37.102 -22.277 1.00 27.73 C

ANISOU 476 CD 1 TYR A 374 3457 4163 2918 250 152 186 C

ATOM 477 CE1 TYR A 374 -5.230 37.240 -22.132 1.00 23.55 C

ANISOU 477 CE1 TYR A 374 2920 3646 2384 257 149 240 C

ATOM 478 CD2 TYR A 374 -3.962 34.976 -21.207 1.00 13.42 C

ANISOU 478 CD2 TYR A 374 1657 2277 1166 227 88 82 C

ATOM 479 CE2 TYR A 374 -5.319 35.107 -21.061 1.00 22.08 C

ANISOU 479 CE2 TYR A 374 2746 3386 2258 234 86 135 C

ATOM 480 CZ TYR A 374 -5.949 36.238 -21.523 1.00 25.43 C

ANISOU 480 CZ TYR A 374 3160 3852 2649 249 116 212 C

ATOM 481 OH TYR A 374 -7.309 36.359 -21.374 1.00 21.23 O

ANISOU 481 OH TYR A 374 2619 3330 2117 255 114 265 O

ATOM 482 C TYR A 374 0.256 36.350 -23.446 1.00 16.73 C

ANISOU 482 C TYR A 374 2055 2774 1529 222 158 -0 C

ATOM 483 0 TYR A 374 0.637 37.518 -23.515 1.00 17.12 0

ANISOU 483 0 TYR A 374 2111 2819 1574 236 198 51 0

ATOM 484 N LYS A 375 1.100 35.323 -23.389 1.00 10.16 N

ANISOU 484 N LYS A 375 1221 1919 721 206 132 -86 N

ATOM 485 CA LYS A 375 2.544 35.555 -23.438 1.00 16.43 C ANISOU 485 CA LYS A 375 2021 2686 1534 204 149 -124 C

ATOM 486 CB LYS A 375 3.317 34.260 -23.142 1.00 16.14 C

ANISOU 486 CB LYS A 375 1984 2610 1539 186 112 -220 C

ATOM 487 CG LYS A 375 3.252 33.883 -21.664 1.00 17.09 C

ANISOU 487 CG LYS A 375 2142 2631 1720 188 89 -226 C

ATOM 488 CD LYS A 375 3.904 32.532 -21.358 1.00 16.68 C

ANISOU 488 CD LYS A 375 2086 2540 1713 171 49 -315 C

ATOM 489 CE LYS A 375 3.544 32.096 -19.939 1.00 18.06 C

ANISOU 489 CE LYS A 375 2294 2629 1938 174 23 -307 C

ATOM 490 NZ LYS A 375 4.081 30.746 -19.584 1.00 23.57 N

ANISOU 490 NZ LYS A 375 2986 3284 2685 159 -17 -384 N

ATOM 491 C LYS A 375 3.005 36.217 -24.744 1.00 21.19 C

ANISOU 491 C LYS A 375 2595 3371 2085 206 183 -109 C

ATOM 492 0 LYS A 375 3.879 37.092 -24.734 1.00 11.93 O

ANISOU 492 O LYS A 375 1431 2176 924 215 219 -89 O

ATOM 493 N GLU A 376 2.413 35.805 -25.861 1.00 17.04 N

ANISOU 493 N GLU A 376 2033 2939 1500 200 173 -117 N

ATOM 494 CA GLU A 376 2.683 36.452 -27.140 1.00 15.41 C

ANISOU 494 CA GLU A 376 1799 2823 1232 204 206 -91 C

ATOM 495 CB GLU A 376 1.955 35.724 -28.273 1.00 29.98 C

ANISOU 495 CB GLU A 376 3605 4773 3013 195 181 -118 C

ATOM 496 CG GLU A 376 2.550 34.370 -28.564 1.00 36.13 C

ANISOU 496 CG GLU A 376 4365 5559 3802 173 148 -229 C

ATOM 497 CD GLU A 376 4.051 34.454 -28.717 1.00 44.59 C

ANISOU 497 CD GLU A 376 5440 6607 4894 167 171 -276 C

ATOM 498 OE1 GLU A 376 4.500 35.061 -29.714 1.00 32.70 O

ANISOU 498 OE1 GLU A 376 3916 5172 3338 171 206 -257 O

ATOM 499 OE2 GLU A 376 4.780 33.937 -27.833 1.00 34.36 O

ANISOU 499 OE2 GLU A 376 4166 5224 3667 159 156 -328 O

ATOM 500 C GLU A 376 2.296 37.921 -27.126 1.00 30.75 C

ANISOU 500 C GLU A 376 3750 4771 3161 226 249 15 C

ATOM 501 O GLU A 376 3.096 38.788 -27.506 1.00 28.14 O

ANISOU 501 O GLU A 376 3417 4448 2825 234 290 42 O

ATOM 502 N ALA A 377 1.074 38.201 -26.680 1.00 19.02 N

ANISOU 502 N ALA A 377 2273 3279 1676 235 241 75 N

ATOM 503 CA ALA A 377 0.556 39.562 -26.707 1.00 18.24 C

ANISOU 503 CA ALA A 377 2177 3189 1566 256 280 178 C

ATOM 504 CB ALA A 377 -0.883 39.610 -26.148 1.00 17.16 C

ANISOU 504 CB ALA A 377 2046 3040 1435 263 264 229 C

ATOM 505 C ALA A 377 1.466 40.517 -25.946 1.00 29.12 C

ANISOU 505 C ALA A 377 3582 4484 2999 266 318 202 C

ATOM 506 O ALA A 377 1.839 41.578 -26.460 1.00 21.04 O

ANISOU 506 O ALA A 377 2548 3483 1963 278 361 256 O

ATOM 507 N ILE A 378 1.837 40.139 -24.725 1.00 29.05 N

ANISOU 507 N ILE A 378 3606 4380 3051 262 300 160 N

ATOM 508 CA ILE A 378 2.660 41.018 -23.905 1.00 24.45 C ANISOU 508 CA ILE A 378 3050 3716 2524 273 331 177 C

ATOM 509 CB ILE A 378 2.768 40.552 -22.435 1.00 25.38 C

ANISOU 509 CB ILE A 378 3207 3735 2703 270 304 139 C

ATOM 510 CG2 ILE A 378 1.412 40.629 -21.753 1.00 22.79 C

ANISOU 510 CG2 ILE A 378 2892 3390 2376 278 293 188 C

ATOM 511 CGI ILE A 378 3.361 39.144 -22.342 1.00 17.83 C

ANISOU 511 CGI ILE A 378 2252 2766 1758 251 261 42 C

ATOM 512 CD1 ILE A 378 3.768 38.755 -20.889 1.00 22.47 C

ANISOU 512 CD 1 ILE A 378 2878 3252 2407 250 237 4 C

ATOM 513 C ILE A 378 4.054 41.242 -24.481 1.00 25.46 C

ANISOU 513 C ILE A 378 3166 3850 2657 269 356 143 C

ATOM 514 O ILE A 378 4.633 42.309 -24.287 1.00 28.65 O

ANISOU 514 O ILE A 378 3576 4219 3092 281 395 180 O

ATOM 515 N ARG A 379 4.597 40.251 -25.186 1.00 27.88 N

ANISOU 515 N ARG A 379 3454 4200 2939 252 334 70 N

ATOM 516 CA ARG A 379 5.879 40.458 -25.843 1.00 30.98 C

ANISOU 516 CA ARG A 379 3832 4607 3332 248 361 39 C

ATOM 517 CB ARG A 379 6.414 39.162 -26.468 1.00 20.59 C

ANISOU 517 CB ARG A 379 2498 3330 1997 227 331 -56 C

ATOM 518 CG ARG A 379 7.774 39.343 -27.139 1.00 22.32 C

ANISOU 518 CG ARG A 379 2700 3561 2219 222 361 -92 C

ATOM 519 CD ARG A 379 8.336 38.035 -27.722 1.00 25.83 C

ANISOU 519 CD ARG A 379 3125 4040 2650 201 332 -193 C

ATOM 520 NE ARG A 379 7.411 37.325 -28.606 1.00 22.78 N

ANISOU 520 NE ARG A 379 2711 3749 2194 193 308 -205 N

ATOM 521 CZ ARG A 379 7.099 37.706 -29.841 1.00 27.78 C

ANISOU 521 CZ ARG A 379 3315 4487 2751 197 333 -169 C

ATOM 522 NH1 ARG A 379 7.617 38.815 -30.349 1.00 34.90 N ANISOU 522 NH1 ARG A 379 4210 5412 3638 210 385 -111 N

ATOM 523 NH2 ARG A 379 6.252 36.987 -30.562 1.00 30.19 N ANISOU 523 NH2 ARG A 379 3597 4877 2998 189 304 -189 N

ATOM 524 C ARG A 379 5.726 41.536 -26.920 1.00 33.84 C

ANISOU 524 C ARG A 379 4168 5045 3647 261 410 117 C

ATOM 525 O ARG A 379 6.399 42.569 -26.891 1.00 33.20 O

ANISOU 525 O ARG A 379 4087 4934 3593 272 453 156 O

ATOM 526 N ILE A 380 4.821 41.277 -27.854 1.00 30.61 N

ANISOU 526 N ILE A 380 3734 4732 3167 260 400 141 N

ATOM 527 CA ILE A 380 4.603 42.132 -29.013 1.00 24.72 C

ANISOU 527 CA ILE A 380 2957 4073 2360 271 439 214 C

ATOM 528 CB ILE A 380 3.457 41.564 -29.888 1.00 27.19 C

ANISOU 528 CB ILE A 380 3245 4491 2595 268 411 224 C

ATOM 529 CG2 ILE A 380 3.176 42.459 -31.085 1.00 26.13 C

ANISOU 529 CG2 ILE A 380 3081 4455 2394 282 449 307 C

ATOM 530 CGI ILE A 380 3.802 40.146 -30.352 1.00 17.24 C

ANISOU 530 CGI ILE A 380 1972 3270 1310 246 371 117 C

ATOM 531 CD 1 ILE A 380 2.602 39.350 -30.848 1.00 26.34 C ANISOU 531 CD1 ILE A 380 3104 4498 2406 240 329 104 C

ATOM 532 C ILE A 380 4.306 43.573 -28.589 1.00 34.97 C ANISOU 532 C ILE A 380 4264 5331 3690 293 481 316 C

ATOM 533 O ILE A 380 4.953 44.505 -29.058 1.00 37.12 O

ANISOU 533 O ILE A 380 4523 5613 3966 303 530 360 O

ATOM 534 N SER A 381 3.341 43.747 -27.689 1.00 32.37 N

ANISOU 534 N SER A 381 3954 4955 3388 300 466 351 N

ATOM 535 C SER A 381 3.297 45.241 -25.741 1.00 35.29 C

ANISOU 535 C SER A 381 4368 5163 3877 323 500 418 C

ATOM 536 O SER A 381 2.485 44.937 -24.880 1.00 31.07 O

ANISOU 536 O SER A 381 3855 4590 3361 323 473 417 O ATOM 537 CA ASER A 381 2.956 45.075 -27.218 0.50 27.89 C ANISOU 537 CA ASER A 381 3394 4346 2858 321 504 443 C ATOM 538 CB ASER A 381 1.457 45.299 -27.436 0.50 26.76 C ANISOU 538 CB ASER A 381 3238 4251 2677 330 494 515 C ATOM 539 OG ASER A 381 1.079 46.622 -27.102 0.50 20.83 O ANISOU 539 OG ASER A 381 2487 3466 1961 350 535 607 O ATOM 540 CA BSER A 381 2.950 45.074 -27.217 0.50 27.91 C ANISOU 540 CA BSER A 381 3396 4348 2860 321 504 443 C ATOM 541 CB BSER A 381 1.444 45.285 -27.408 0.50 26.63 C ANISOU 541 CB BSER A 381 3223 4234 2662 330 493 514 C ATOM 542 OG BSER A 381 1.008 44.827 -28.677 0.50 29.86 O ANISOU 542 OG BSER A 381 3599 4757 2988 325 480 518 O

ATOM 543 N PRO A 382 4.509 45.737 -25.444 1.00 31.66 N

ANISOU 543 N PRO A 382 3916 4645 3468 325 528 398 N

ATOM 544 CD PRO A 382 5.501 46.233 -26.409 1.00 38.98 C

ANISOU 544 CD PRO A 382 4816 5609 4383 326 568 407 C

ATOM 545 CA PRO A 382 4.982 45.857 -24.061 1.00 26.27 C

ANISOU 545 CA PRO A 382 3268 3852 2861 326 521 364 C

ATOM 546 CB PRO A 382 6.455 46.266 -24.222 1.00 25.88 C

ANISOU 546 CB PRO A 382 3211 3770 2850 326 551 334 C

ATOM 547 CG PRO A 382 6.784 46.049 -25.676 1.00 37.53 C

ANISOU 547 CG PRO A 382 4653 5342 4266 319 567 335 C

ATOM 548 C PRO A 382 4.248 46.909 -23.233 1.00 30.96 C

ANISOU 548 C PRO A 382 3874 4393 3495 344 543 435 C

ATOM 549 O PRO A 382 4.460 46.975 -22.020 1.00 31.14 O

ANISOU 549 O PRO A 382 3928 4330 3574 346 534 407 O

ATOM 550 N THR A 383 3.417 47.727 -23.871 1.00 35.37 N

ANISOU 550 N THR A 383 4409 5002 4027 357 573 524 N

ATOM 551 CA THR A 383 2.621 48.713 -23.145 1.00 37.91 C

ANISOU 551 CA THR A 383 4739 5276 4389 373 595 593 C

ATOM 552 CB THR A 383 2.671 50.107 -23.827 1.00 33.57 C

ANISOU 552 CB THR A 383 4156 4746 3852 391 653 685 C ATOM 553 OG1 THR A 383 2.054 50.036 -25.119 1.00 26.57 O ANISOU 553 OG1 THR A 383 3238 3966 2893 392 656 737 O ATOM 554 CG2 THR A 383 4.116 50.603 -23.977 1.00 17.96 C ANISOU 554 CG2 THR A 383 2172 2734 1917 391 687 661 C

ATOM 555 C THR A 383 1.170 48.235 -23.038 1.00 42.06 C

ANISOU 555 C THR A 383 5267 5836 4877 373 564 619 C

ATOM 556 O THR A 383 0.273 48.996 -22.671 1.00 50.09 O

ANISOU 556 O THR A 383 6283 6835 5914 386 582 686 O

ATOM 557 N PHE A 384 0.963 46.963 -23.366 1.00 32.71 N

ANISOU 557 N PHE A 384 4084 4699 3645 357 519 564 N

ATOM 558 CA PHE A 384 -0.353 46.324 -23.363 1.00 38.39 C

ANISOU 558 CA PHE A 384 4802 5455 4329 354 485 576 C

ATOM 559 CB PHE A 384 -0.296 45.057 -24.230 1.00 39.86 C

ANISOU 559 CB PHE A 384 4973 5717 4455 336 446 516 C

ATOM 560 CG PHE A 384 -1.620 44.635 -24.808 1.00 35.31 C

ANISOU 560 CG PHE A 384 4376 5215 3827 335 421 547 C

ATOM 561 CD 1 PHE A 384 -1.675 43.615 -25.747 1.00 35.05 C ANISOU 561 CD 1 PHE A 384 4320 5262 3734 321 389 499 C

ATOM 562 CD2 PHE A 384 -2.801 45.255 -24.429 1.00 38.72 C ANISOU 562 CD2 PHE A 384 4807 5635 4271 348 430 620 C

ATOM 563 CE1 PHE A 384 -2.880 43.216 -26.296 1.00 37.46 C

ANISOU 563 CE1 PHE A 384 4603 5636 3993 320 363 523 C

ATOM 564 CE2 PHE A 384 -4.017 44.859 -24.972 1.00 32.58 C

ANISOU 564 CE2 PHE A 384 4007 4924 3448 348 405 647 C

ATOM 565 CZ PHE A 384 -4.057 43.839 -25.904 1.00 42.00 C

ANISOU 565 CZ PHE A 384 5178 6198 4582 334 371 598 C

ATOM 566 C PHE A 384 -0.755 45.929 -21.943 1.00 24.90 C

ANISOU 566 C PHE A 384 3132 3665 2665 352 461 546 C

ATOM 567 O PHE A 384 -0.714 44.743 -21.589 1.00 26.63 O

ANISOU 567 O PHE A 384 3366 3874 2878 338 418 477 O

ATOM 568 N ALA A 385 -1.153 46.905 -21.131 1.00 22.83 N

ANISOU 568 N ALA A 385 2882 3344 2448 367 489 598 N

ATOM 569 CA ALA A 385 -1.517 46.613 -19.745 1.00 20.97 C

ANISOU 569 CA ALA A 385 2684 3033 2252 368 471 572 C

ATOM 570 CB ALA A 385 -1.827 47.897 -18.989 1.00 29.87 C

ANISOU 570 CB ALA A 385 3818 4100 3432 386 510 629 C

ATOM 571 C ALA A 385 -2.680 45.624 -19.657 1.00 22.46 C

ANISOU 571 C ALA A 385 2874 3250 2410 360 432 565 C

ATOM 572 O ALA A 385 -2.727 44.766 -18.768 1.00 16.20 O

ANISOU 572 O ALA A 385 2109 2413 1632 351 400 514 O

ATOM 573 N ASP A 386 -3.608 45.737 -20.601 1.00 13.85 N

ANISOU 573 N ASP A 386 1751 2234 1277 362 433 619 N

ATOM 574 CA ASP A 386 -4.814 44.921 -20.606 1.00 21.66 C

ANISOU 574 CA ASP A 386 2734 3253 2242 356 399 620 C

ATOM 575 CB ASP A 386 -5.689 45.285 -21.804 1.00 28.20 C

ANISOU 575 CB ASP A 386 3516 4167 3031 364 402 681 C

ATOM 576 CG ASP A 386 -6.981 45.954 -21.397 1.00 49.74 C

ANISOU 576 CG ASP A 386 6230 6874 5794 380 410 744 C

ATOM 577 OD1 ASP A 386 -7.203 47.121 -21.792 1.00 55.40 O ANISOU 577 OD1 ASP A 386 6920 7601 6528 399 441 811 O

ATOM 578 OD2 ASP A 386 -7.775 45.308 -20.680 1.00 60.25 O

ANISOU 578 OD2 ASP A 386 7576 8178 7138 376 387 728 O

ATOM 579 C ASP A 386 -4.450 43.454 -20.663 1.00 24.58 C

ANISOU 579 C ASP A 386 3111 3636 2593 336 353 534 C

ATOM 580 O ASP A 386 -5.095 42.616 -20.038 1.00 19.92 O

ANISOU 580 O ASP A 386 2534 3023 2011 330 322 508 O

ATOM 581 N ALA A 387 -3.405 43.142 -21.415 1.00 18.10 N

ANISOU 581 N ALA A 387 2278 2849 1749 327 348 488 N

ATOM 582 CA ALA A 387 -3.004 41.752 -21.591 1.00 19.43 C

ANISOU 582 CA ALA A 387 2447 3034 1904 308 305 403 C

ATOM 583 CB ALA A 387 -2.044 41.606 -22.773 1.00 23.17 C

ANISOU 583 CB ALA A 387 2894 3570 2339 300 308 369 C

ATOM 584 C ALA A 387 -2.380 41.208 -20.309 1.00 17.05 C

ANISOU 584 C ALA A 387 2185 2642 1653 303 288 345 C

ATOM 585 O ALA A 387 -2.625 40.064 -19.928 1.00 17.20 O

ANISOU 585 O ALA A 387 2212 2647 1678 291 249 295 O

ATOM 586 N TYR A 388 -1.571 42.025 -19.645 1.00 16.85 N

ANISOU 586 N TYR A 388 2182 2553 1665 312 315 351 N

ATOM 587 CA TYR A 388 -1.027 41.640 -18.344 1.00 19.96 C

ANISOU 587 CA TYR A 388 2616 2862 2107 310 300 304 C

ATOM 588 CB TYR A 388 -0.096 42.720 -17.783 1.00 12.04 C

ANISOU 588 CB TYR A 388 1631 1800 1143 322 334 314 C

ATOM 589 CG TYR A 388 1.328 42.563 -18.280 1.00 15.42 C

ANISOU 589 CG TYR A 388 2052 2231 1577 314 334 259 C

ATOM 590 CD1 TYR A 388 2.197 41.673 -17.661 1.00 19.68 C

ANISOU 590 CD 1 TYR A 388 2612 2723 2142 304 301 182 C

ATOM 591 CE1 TYR A 388 3.499 41.502 -18.114 1.00 22.67 C

ANISOU 591 CE1 TYR A 388 2981 3101 2530 296 301 130 C

ATOM 592 CD2 TYR A 388 1.798 43.294 -19.371 1.00 12.17 C

ANISOU 592 CD2 TYR A 388 1610 1867 1147 318 367 286 C

ATOM 593 CE2 TYR A 388 3.102 43.132 -19.833 1.00 17.59 C

ANISOU 593 CE2 TYR A 388 2288 2556 1841 310 370 235 C

ATOM 594 CZ TYR A 388 3.950 42.240 -19.199 1.00 19.65 C

ANISOU 594 CZ TYR A 388 2570 2767 2130 299 337 155 C

ATOM 595 OH TYR A 388 5.247 42.066 -19.657 1.00 20.05 O

ANISOU 595 OH TYR A 388 2609 2816 2192 291 340 102 O

ATOM 596 C TYR A 388 -2.141 41.333 -17.350 1.00 18.40 C

ANISOU 596 C TYR A 388 2440 2628 1924 314 285 324 C

ATOM 597 O TYR A 388 -2.111 40.296 -16.680 1.00 13.47 O

ANISOU 597 O TYR A 388 1835 1971 1314 304 251 275 O

ATOM 598 N SER A 389 -3.118 42.237 -17.278 1.00 18.48 N

ANISOU 598 N SER A 389 2445 2644 1932 327 314 398 N

ATOM 599 CA SER A 389 -4.247 42.123 -16.365 1.00 11.88 C

ANISOU 599 CA SER A 389 1627 1775 1111 333 309 427 C

ATOM 600 CB SER A 389 -5.169 43.338 -16.520 1.00 20.46 C ANISOU 600 CB SER A 389 2699 2876 2199 349 348 512 C

ATOM 601 OG SER A 389 -6.267 43.234 -15.633 1.00 20.07 O

ANISOU 601 OG SER A 389 2662 2791 2172 355 345 533 O

ATOM 602 C SER A 389 -5.047 40.862 -16.662 1.00 15.12 C

ANISOU 602 C SER A 389 2023 2222 1500 319 270 404 C

ATOM 603 O SER A 389 -5.349 40.076 -15.766 1.00 18.27 O

ANISOU 603 O SER A 389 2445 2579 1919 315 247 378 O

ATOM 604 N ASN A 390 -5.405 40.689 -17.926 1.00 19.95 N

ANISOU 604 N ASN A 390 2595 2914 2071 313 262 414 N

ATOM 605 CA ASN A 390 -6.121 39.500 -18.348 1.00 13.87 C

ANISOU 605 CA ASN A 390 1804 2185 1282 300 224 386 C

ATOM 606 CB ASN A 390 -6.582 39.628 -19.802 1.00 16.08 C

ANISOU 606 CB ASN A 390 2038 2562 1511 298 222 410 C

ATOM 607 CG ASN A 390 -7.834 40.481 -19.929 1.00 26.40 C

ANISOU 607 CG ASN A 390 3330 3890 2810 312 244 496 C ATOM 608 OD1 ASN A 390 -8.733 40.385 -19.103 1.00 27.32 O ANISOU 608 OD1 ASN A 390 3459 3966 2954 316 243 519 O ATOM 609 ND2 ASN A 390 -7.895 41.310 -20.960 1.00 22.43 N ANISOU 609 ND2 ASN A 390 2798 3451 2272 321 266 545 N

ATOM 610 C ASN A 390 -5.313 38.234 -18.120 1.00 21.92 C

ANISOU 610 C ASN A 390 2833 3181 2314 283 186 300 C

ATOM 611 O ASN A 390 -5.854 37.241 -17.677 1.00 13.95 O

ANISOU 611 O ASN A 390 1826 2153 1320 275 157 274 O

ATOM 612 N MET A 391 -4.012 38.262 -18.405 1.00 13.32 N

ANISOU 612 N MET A 391 1747 2089 1225 279 188 256 N

ATOM 613 CA MET A 391 -3.195 37.092 -18.113 1.00 8.34 C

ANISOU 613 CA MET A 391 1125 1429 615 264 154 175 C

ATOM 614 CB MET A 391 -1.765 37.323 -18.585 1.00 13.15 C

ANISOU 614 CB MET A 391 1732 2043 1222 260 163 134 C

ATOM 615 CG MET A 391 -0.806 36.190 -18.285 1.00 21.42 C

ANISOU 615 CG MET A 391 2788 3055 2298 245 129 50 C

ATOM 616 SD MET A 391 0.830 36.473 -19.036 1.00 19.87 S

ANISOU 616 SD MET A 391 2579 2872 2097 240 143 2 S

ATOM 617 CE MET A 391 1.831 35.449 -18.017 1.00 10.78 C

ANISOU 617 CE MET A 391 1454 1640 1001 230 107 -75 C

ATOM 618 C MET A 391 -3.217 36.827 -16.611 1.00 17.67 C

ANISOU 618 C MET A 391 2349 2524 1842 268 145 169 C

ATOM 619 O MET A 391 -3.251 35.686 -16.164 1.00 15.26 O

ANISOU 619 O MET A 391 2049 2192 1557 257 111 124 O

ATOM 620 N GLY A 392 -3.203 37.893 -15.825 1.00 10.92 N

ANISOU 620 N GLY A 392 1522 1624 1002 284 177 214 N

ATOM 621 CA GLY A 392 -3.318 37.741 -14.387 1.00 19.27 C

ANISOU 621 CA GLY A 392 2621 2606 2095 290 171 214 C

ATOM 622 C GLY A 392 -4.570 36.968 -13.978 1.00 18.78 C

ANISOU 622 C GLY A 392 2558 2541 2036 287 153 230 C

ATOM 623 O GLY A 392 -4.489 36.071 -13.149 1.00 14.73 O ANISOU 623 O GLY A 392 2065 1984 1548 282 128 199 O

ATOM 624 N ASN A 393 -5.721 37.322 -14.548 1.00 14.23 N

ANISOU 624 N ASN A 393 1956 2010 1439 290 167 282 N

ATOM 625 CA ASN A 393 -6.966 36.598 -14.305 1.00 12.91 C

ANISOU 625 CA ASN A 393 1781 1846 1279 286 151 298 C

ATOM 626 CB ASN A 393 -8.082 37.156 -15.180 1.00 14.75 C

ANISOU 626 CB ASN A 393 1979 2140 1486 291 167 355 C

ATOM 627 CG ASN A 393 -8.565 38.506 -14.713 1.00 16.23 C

ANISOU 627 CG ASN A 393 2181 2307 1678 310 210 426 C

ATOM 628 OD1 ASN A 393 -9.290 39.194 -15.419 1.00 19.73 O

ANISOU 628 OD1 ASN A 393 2598 2797 2103 316 228 478 O

ATOM 629 ND2 ASN A 393 -8.138 38.903 -13.529 1.00 16.88 N

ANISOU 629 ND2 ASN A 393 2305 2322 1787 319 227 426 N

ATOM 630 C ASN A 393 -6.831 35.110 -14.591 1.00 12.57 C

ANISOU 630 C ASN A 393 1719 1812 1244 268 107 235 C

ATOM 631 O ASN A 393 -7.371 34.268 -13.870 1.00 13.26 O

ANISOU 631 O ASN A 393 1816 1865 1358 264 89 227 O

ATOM 632 N THR A 394 -6.124 34.778 -15.660 1.00 16.90 N

ANISOU 632 N THR A 394 2240 2410 1772 257 91 189 N

ATOM 633 CA THR A 394 -5.951 33.372 -16.011 1.00 13.15 C

ANISOU 633 CA THR A 394 1742 1945 1309 238 50 122 C

ATOM 634 CB THR A 394 -5.415 33.225 -17.450 1.00 18.61 C

ANISOU 634 CB THR A 394 2393 2712 1965 227 41 82 C

ATOM 635 OGl THR A 394 -6.431 33.651 -18.371 1.00 15.68 O

ANISOU 635 OGl THR A 394 1989 2413 1555 230 50 125 O

ATOM 636 CG2 THR A 394 -5.070 31.764 -17.742 1.00 18.18 C

ANISOU 636 CG2 THR A 394 2316 2661 1932 207 -1 1 C

ATOM 637 C THR A 394 -5.063 32.634 -14.990 1.00 10.53 C

ANISOU 637 C THR A 394 1441 1540 1019 234 30 75 C

ATOM 638 0 THR A 394 -5.374 31.514 -14.561 1.00 14.03 O

ANISOU 638 O THR A 394 1881 1956 1494 224 2 48 O

ATOM 639 N LEU A 395 -3.964 33.257 -14.577 1.00 11.38 N

ANISOU 639 N LEU A 395 1578 1615 1131 241 44 66 N

ATOM 640 CA LEU A 395 -3.117 32.644 -13.547 1.00 9.74 C

ANISOU 640 CA LEU A 395 1402 1338 962 239 24 27 C

ATOM 641 CB LEU A 395 -1.859 33.462 -13.305 1.00 8.53 C

ANISOU 641 CB LEU A 395 1272 1157 810 247 40 14 C

ATOM 642 CG LEU A 395 -0.905 33.513 -14.503 1.00 20.12 C

ANISOU 642 CG LEU A 395 2710 2672 2261 237 40 -29 C

ATOM 643 CD1 LEU A 395 0.330 34.367 -14.184 1.00 13.62 C

ANISOU 643 CD 1 LEU A 395 1911 1815 1449 245 58 -39 C

ATOM 644 CD2 LEU A 395 -0.514 32.110 -14.934 1.00 13.85 C

ANISOU 644 CD2 LEU A 395 1891 1886 1486 217 -0 -101 C

ATOM 645 C LEU A 395 -3.872 32.470 -12.236 1.00 12.99 C

ANISOU 645 C LEU A 395 1846 1693 1396 248 25 63 C

ATOM 646 0 LEU A 395 -3.688 31.480 -11.525 1.00 15.19 O ANISOU 646 O LEU A 395 2136 1927 1707 242 -3 35 O

ATOM 647 N LYS A 396 -4.699 33.446 -11.897 1.00 11.58 N

ANISOU 647 N LYS A 396 1682 1516 1203 262 57 128 N

ATOM 648 CA LYS A 396 -5.517 33.332 -10.691 1.00 15.92 C

ANISOU 648 CA LYS A 396 2261 2018 1770 271 63 166 C

ATOM 649 CB LYS A 396 -6.370 34.586 -10.499 1.00 14.14 C

ANISOU 649 CB LYS A 396 2044 1800 1527 287 105 235 C

ATOM 650 CG LYS A 396 -7.120 34.657 -9.156 1.00 24.64 C

ANISOU 650 CG LYS A 396 3411 3080 2873 299 120 274 C

ATOM 651 CD LYS A 396 -8.036 35.881 -9.114 1.00 24.49 C

ANISOU 651 CD LYS A 396 3393 3073 2841 313 163 340 C

ATOM 652 CE LYS A 396 -8.976 35.862 -7.915 1.00 35.37 C

ANISOU 652 CE LYS A 396 4798 4409 4232 323 179 379 C

ATOM 653 NZ LYS A 396 -8.243 35.830 -6.625 1.00 44.62 N

ANISOU 653 NZ LYS A 396 6015 5524 5414 331 178 358 N

ATOM 654 C LYS A 396 -6.396 32.083 -10.776 1.00 20.13 C

ANISOU 654 C LYS A 396 2769 2556 2322 259 37 157 C

ATOM 655 O LYS A 396 -6.531 31.339 -9.802 1.00 14.97 O

ANISOU 655 O LYS A 396 2136 1853 1697 260 23 154 O

ATOM 656 N GLU A 397 -6.973 31.846 -11.948 1.00 16.08 N

ANISOU 656 N GLU A 397 2211 2104 1796 249 30 152 N

ATOM 657 CA GLU A 397 -7.858 30.704 -12.124 1.00 23.98 C

ANISOU 657 CA GLU A 397 3182 3112 2819 238 5 141 C

ATOM 658 CB GLU A 397 -8.651 30.818 -13.425 1.00 26.51 C

ANISOU 658 CB GLU A 397 3453 3507 3112 231 5 149 C

ATOM 659 CG GLU A 397 -9.688 29.727 -13.597 1.00 40.12 C ANISOU 659 CG GLU A 397 5142 5238 4863 220 -19 139 C

ATOM 660 CD GLU A 397 -10.655 30.005 -14.724 1.00 37.52 C

ANISOU 660 CD GLU A 397 4768 4982 4505 218 -17 159 C

ATOM 661 OE1 GLU A 397 -10.672 31.149 -15.234 1.00 38.52 O ANISOU 661 OE1 GLU A 397 4895 5150 4591 228 8 196 O

ATOM 662 OE2 GLU A 397 -11.403 29.074 -15.091 1.00 36.24 O ANISOU 662 OE2 GLU A 397 4568 4836 4365 207 -42 137 O

ATOM 663 C GLU A 397 -7.062 29.404 -12.066 1.00 28.49 C

ANISOU 663 C GLU A 397 3744 3658 3424 223 -33 72 C

ATOM 664 O GLU A 397 -7.578 28.370 -11.649 1.00 20.19 O

ANISOU 664 O GLU A 397 2683 2578 2410 216 -53 63 O

ATOM 665 N MET A 398 -5.794 29.472 -12.462 1.00 16.17 N

ANISOU 665 N MET A 398 2184 2103 1855 218 -42 24 N

ATOM 666 CA MET A 398 -4.903 28.317 -12.407 1.00 21.78 C ANISOU 666 CA MET A 398 2887 2786 2603 204 -78 -43 C

ATOM 667 CB MET A 398 -3.768 28.481 -13.417 1.00 24.59 C ANISOU 667 CB MET A 398 3223 3180 2939 196 -83 -97 C

ATOM 668 CG MET A 398 -4.241 28.558 -14.853 1.00 20.27 C ANISOU 668 CG MET A 398 2628 2715 2356 187 -82 -109 C

ATOM 669 SD MET A 398 -2.875 28.923 -15.960 1.00 19.31 S ANISOU 669 SD MET A 398 2490 2640 2206 180 -78 -162 S

ATOM 670 CE MET A 398 -1.949 27.390 -15.876 1.00 21.68 C

ANISOU 670 CE MET A 398 2773 2902 2562 161 -121 -254 C

ATOM 671 C MET A 398 -4.324 28.109 -11.014 1.00 19.17 C

ANISOU 671 C MET A 398 2603 2379 2303 212 -84 -39 C

ATOM 672 O MET A 398 -3.533 27.189 -10.789 1.00 25.02 O

ANISOU 672 O MET A 398 3341 3087 3080 203 -113 -88 O

ATOM 673 N GLN A 399 -4.718 28.968 -10.080 1.00 18.24 N

ANISOU 673 N GLN A 399 2525 2234 2172 230 -56 19 N

ATOM 674 CA GLN A 399 -4.257 28.891 -8.695 1.00 20.46 C

ANISOU 674 CA GLN A 399 2854 2449 2472 241 -60 30 C

ATOM 675 CB GLN A 399 -4.465 27.487 -8.102 1.00 26.71 C

ANISOU 675 CB GLN A 399 3639 3198 3309 233 -91 14 C

ATOM 676 CG GLN A 399 -5.831 26.872 -8.351 1.00 42.24 C

ANISOU 676 CG GLN A 399 5576 5182 5293 226 -90 39 C

ATOM 677 CD GLN A 399 -6.846 27.246 -7.295 1.00 60.02 C

ANISOU 677 CD GLN A 399 7859 7406 7540 241 -63 108 C

ATOM 678 OEl GLN A 399 -6.656 28.204 -6.546 1.00 69.11 O

ANISOU 678 OEl GLN A 399 9053 8540 8665 258 -39 141 O

ATOM 679 NE2 GLN A 399 -7.936 26.487 -7.227 1.00 65.38 N

ANISOU 679 NE2 GLN A 399 8514 8080 8247 236 -66 128 N

ATOM 680 C GLN A 399 -2.792 29.280 -8.562 1.00 29.41 C

ANISOU 680 C GLN A 399 4008 3563 3603 244 -67 -8 C

ATOM 681 O GLN A 399 -2.133 28.890 -7.594 1.00 22.44 O

ANISOU 681 O GLN A 399 3154 2628 2743 249 -84 -22 O

ATOM 682 N ASP A 400 -2.275 30.024 -9.539 1.00 23.76 N

ANISOU 682 N ASP A 400 3275 2890 2862 242 -53 -25 N

ATOM 683 CA ASP A 400 -0.947 30.612 -9.422 1.00 22.42 C

ANISOU 683 CA ASP A 400 3125 2703 2691 246 -51 -54 C

ATOM 684 CB ASP A 400 -0.271 30.672 -10.790 1.00 15.81 C

ANISOU 684 CB ASP A 400 2249 1915 1842 234 -53 -98 C

ATOM 685 CG ASP A 400 1.141 31.255 -10.734 1.00 24.31 C

ANISOU 685 CG ASP A 400 3341 2972 2925 238 -50 -131 C

ATOM 686 OD1 ASP A 400 1.635 31.582 -9.629 1.00 22.89 O

ANISOU 686 OD1 ASP A 400 3200 2739 2758 250 -51 -124 O

ATOM 687 OD2 ASP A 400 1.760 31.396 -11.812 1.00 16.55 O

ANISOU 687 OD2 ASP A 400 2329 2028 1931 229 -45 -164 O

ATOM 688 C ASP A 400 -1.121 32.016 -8.845 1.00 26.80 C

ANISOU 688 C ASP A 400 3714 3249 3222 266 -14 -3 C

ATOM 689 O ASP A 400 -1.249 32.983 -9.590 1.00 21.53 O

ANISOU 689 O ASP A 400 3032 2620 2527 269 15 18 O

ATOM 690 N VAL A 401 -1.148 32.117 -7.516 1.00 19.04 N

ANISOU 690 N VAL A 401 2774 2214 2248 279 -13 18 N

ATOM 691 CA VAL A 401 -1.448 33.377 -6.834 1.00 23.03 C

ANISOU 691 CA VAL A 401 3310 2706 2733 298 23 64 C

ATOM 692 CB VAL A 401 -1.804 33.163 -5.336 1.00 25.89 C ANISOU 692 CB VAL A 401 3716 3019 3101 311 19 89 C

ATOM 693 CGI VAL A 401 -1.572 34.443 -4.560 1.00 44.25 C

ANISOU 693 CGI VAL A 401 6078 5323 5413 330 49 110 C

ATOM 694 CG2 VAL A 401 -3.267 32.713 -5.181 1.00 21.38 C

ANISOU 694 CG2 VAL A 401 3138 2458 2528 310 29 136 C

ATOM 695 C VAL A 401 -0.352 34.441 -6.954 1.00 16.43 C

ANISOU 695 C VAL A 401 2484 1865 1893 305 38 46 C

ATOM 696 O VAL A 401 -0.645 35.616 -7.176 1.00 18.35 O

ANISOU 696 O VAL A 401 2727 2126 2121 315 75 80 O

ATOM 697 N GLN A 402 0.900 34.022 -6.816 1.00 18.74 N

ANISOU 697 N GLN A 402 2782 2131 2206 301 10 -8 N

ATOM 698 CA GLN A 402 2.039 34.914 -6.976 1.00 26.34 C

ANISOU 698 CA GLN A 402 3749 3085 3174 306 21 -33 C

ATOM 699 CB GLN A 402 3.342 34.213 -6.595 1.00 22.13 C

ANISOU 699 CB GLN A 402 3225 2513 2671 302 -18 -94 C

ATOM 700 CG GLN A 402 3.603 34.129 -5.106 1.00 30.10 C

ANISOU 700 CG GLN A 402 4279 3467 3689 316 -36 -93 C

ATOM 701 CD GLN A 402 5.040 33.736 -4.798 1.00 43.99 C

ANISOU 701 CD GLN A 402 6037 5205 5470 306 -73 -144 C

ATOM 702 OEl GLN A 402 5.851 33.524 -5.704 1.00 53.03 O ANISOU 702 OEl GLN A 402 7151 6365 6634 293 -83 -184 O

ATOM 703 NE2 GLN A 402 5.359 33.636 -3.517 1.00 53.36 N

ANISOU 703 NE2 GLN A 402 7253 6368 6652 310 -96 -139 N

ATOM 704 C GLN A 402 2.160 35.392 -8.409 1.00 14.47 C

ANISOU 704 C GLN A 402 2205 1635 1658 298 43 -36 C

ATOM 705 O GLN A 402 2.430 36.569 -8.661 1.00 14.71 O

ANISOU 705 O GLN A 402 2234 1672 1682 307 75 -19 O

ATOM 706 N GLY A 403 1.987 34.468 -9.343 1.00 11.54 N

ANISOU 706 N GLY A 403 1799 1301 1284 281 24 -58 N

ATOM 707 CA GLY A 403 2.072 34.826 -10.744 1.00 18.07 C

ANISOU 707 CA GLY A 403 2587 2187 2092 273 42 -62 C

ATOM 708 C GLY A 403 1.064 35.908 -11.084 1.00 11.65 C

ANISOU 708 C GLY A 403 1767 1409 1250 283 84 5 C

ATOM 709 O GLY A 403 1.398 36.868 -11.778 1.00 15.20 O

ANISOU 709 O GLY A 403 2202 1885 1688 287 113 19 O

ATOM 710 N ALA A 404 -0.173 35.740 -10.611 1.00 11.95 N

ANISOU 710 N ALA A 404 1814 1446 1279 287 86 48 N

ATOM 711 CA ALA A 404 -1.256 36.659 -10.959 1.00 17.11 C

ANISOU 711 CA ALA A 404 2457 2134 1909 296 123 112 C

ATOM 712 CB ALA A 404 -2.620 36.174 -10.400 1.00 13.07 C

ANISOU 712 CB ALA A 404 1952 1617 1396 298 118 150 C

ATOM 713 C ALA A 404 -0.928 38.010 -10.398 1.00 13.17 C

ANISOU 713 C ALA A 404 1982 1605 1417 313 158 141 C

ATOM 714 0 ALA A 404 -1.104 39.024 -11.051 1.00 13.31 O

ANISOU 714 O ALA A 404 1982 1653 1422 319 192 177 O

ATOM 715 N LEU A 405 -0.463 38.028 -9.159 1.00 9.62 N ANISOU 715 N LEU A 405 1572 1097 988 322 150 125 N

ATOM 716 CA LEU A 405 -0.118 39.290 -8.532 1.00 14.50 C

ANISOU 716 CA LEU A 405 2211 1681 1616 338 181 143 C

ATOM 717 CB LEU A 405 0.327 39.088 -7.093 1.00 21.91 C

ANISOU 717 CB LEU A 405 3194 2558 2571 347 163 119 C

ATOM 718 CG LEU A 405 0.310 40.383 -6.290 1.00 23.59 C

ANISOU 718 CG LEU A 405 3431 2739 2793 366 198 143 C

ATOM 719 CD1 LEU A 405 -0.291 40.129 -4.925 1.00 29.94 C

ANISOU 719 CD 1 LEU A 405 4275 3509 3593 376 192 156 C ATOM 720 CD2 LEU A 405 1.711 40.991 -6.183 1.00 33.79 C

ANISOU 720 CD2 LEU A 405 4728 4002 4110 371 198 101 C

ATOM 721 C LEU A 405 0.984 39.986 -9.314 1.00 19.82 C

ANISOU 721 C LEU A 405 2865 2366 2299 338 196 122 C

ATOM 722 O LEU A 405 0.949 41.203 -9.509 1.00 20.52 O

ANISOU 722 O LEU A 405 2947 2457 2391 348 235 156 O

ATOM 723 N GLN A 406 1.977 39.218 -9.740 1.00 20.92 N

ANISOU 723 N GLN A 406 2994 2507 2446 325 166 65 N

ATOM 724 CA GLN A 406 3.051 39.782 -10.547 1.00 14.34 C

ANISOU 724 CA GLN A 406 2140 1687 1623 323 181 42 C

ATOM 725 CB GLN A 406 4.045 38.686 -10.944 1.00 22.79 C

ANISOU 725 CB GLN A 406 3198 2758 2703 307 143 -26 C

ATOM 726 CG GLN A 406 5.293 39.181 -11.637 1.00 40.48 C

ANISOU 726 CG GLN A 406 5419 5001 4960 304 157 -58 C

ATOM 727 CD GLN A 406 6.273 39.881 -10.696 1.00 40.85 C

ANISOU 727 CD GLN A 406 5493 4985 5045 316 161 -79 C ATOM 728 OEl GLN A 406 7.338 40.343 -11.135 1.00 19.13 O

ANISOU 728 OEl GLN A 406 2727 2226 2316 316 174 -105 O ATOM 729 NE2 GLN A 406 5.922 39.963 -9.396 1.00 15.58 N

ANISOU 729 NE2 GLN A 406 2329 1738 1852 328 151 -69 N

ATOM 730 C GLN A 406 2.447 40.454 -11.782 1.00 15.91 C

ANISOU 730 C GLN A 406 2302 1948 1796 322 216 90 C

ATOM 731 0 GLN A 406 2.832 41.555 -12.141 1.00 14.27 O

ANISOU 731 O GLN A 406 2082 1742 1596 331 251 112 O

ATOM 732 N CYS A 407 1.470 39.805 -12.407 1.00 6.37 N

ANISOU 732 N CYS A 407 1073 789 557 313 206 110 N

ATOM 733 CA CYS A 407 0.878 40.359 -13.627 1.00 5.82 C

ANISOU 733 CA CYS A 407 967 787 457 313 234 155 C

ATOM 734 CB CYS A 407 -0.005 39.323 -14.345 1.00 17.98 C

ANISOU 734 CB CYS A 407 2482 2383 1966 300 208 153 C

ATOM 735 SG CYS A 407 0.916 37.936 -15.148 1.00 16.26 S

ANISOU 735 SG CYS A 407 2241 2193 1744 277 167 69 S

ATOM 736 C CYS A 407 0.083 41.627 -13.378 1.00 9.23 C

ANISOU 736 C CYS A 407 1403 1215 891 330 275 228 C

ATOM 737 O CYS A 407 0.125 42.560 -14.182 1.00 12.62 O

ANISOU 737 O CYS A 407 1806 1676 1312 336 309 266 O

ATOM 738 N TYR A 408 -0.689 41.655 -12.289 1.00 14.09 N ANISOU 738 N TYR A 408 2046 1791 1517 338 275 250 N

ATOM 739 CA TYR A 408 -1.475 42.852 -11.977 1.00 10.80 C

ANISOU 739 CA TYR A 408 1632 1365 1108 355 316 315 C

ATOM 740 CB TYR A 408 -2.428 42.608 -10.799 1.00 12.06 C

ANISOU 740 CB TYR A 408 1821 1487 1274 361 311 332 C

ATOM 741 CG TYR A 408 -3.475 41.545 -11.038 1.00 10.11 C

ANISOU 741 CG TYR A 408 1564 1274 1004 350 285 341 C

ATOM 742 CD1 TYR A 408 -4.139 41.441 -12.267 1.00 16.43 C

ANISOU 742 CD 1 TYR A 408 2323 2141 1777 344 287 369 C

ATOM 743 CE1 TYR A 408 -5.099 40.458 -12.479 1.00 11.77 C

ANISOU 743 CE1 TYR A 408 1721 1580 1172 334 262 372 C

ATOM 744 CD2 TYR A 408 -3.833 40.657 -10.022 1.00 8.41 C ANISOU 744 CD2 TYR A 408 1377 1023 796 348 260 322 C

ATOM 745 CE2 TYR A 408 -4.790 39.689 -10.226 1.00 14.29 C

ANISOU 745 CE2 TYR A 408 2108 1792 1528 339 239 330 C

ATOM 746 CZ TYR A 408 -5.431 39.602 -11.449 1.00 15.59 C

ANISOU 746 CZ TYR A 408 2231 2021 1670 332 239 353 C

ATOM 747 OH TYR A 408 -6.382 38.628 -11.630 1.00 19.70 O

ANISOU 747 OH TYR A 408 2737 2565 2185 322 216 356 O

ATOM 748 C TYR A 408 -0.530 43.996 -11.628 1.00 10.15 C

ANISOU 748 C TYR A 408 1559 1241 1059 366 346 312 C

ATOM 749 O TYR A 408 -0.763 45.130 -11.971 1.00 9.51 O

ANISOU 749 O TYR A 408 1460 1167 986 377 386 361 O

ATOM 750 N THR A 409 0.556 43.667 -10.947 1.00 12.90 N

ANISOU 750 N THR A 409 1931 1542 1428 365 325 252 N

ATOM 751 CA THR A 409 1.532 44.651 -10.546 1.00 13.67 C

ANISOU 751 CA THR A 409 2036 1595 1562 375 347 238 C

ATOM 752 CB THR A 409 2.598 44.002 -9.632 1.00 12.41 C

ANISOU 752 CB THR A 409 1909 1384 1423 372 311 167 C

ATOM 753 OGl THR A 409 1.961 43.519 -8.451 1.00 14.45 O ANISOU 753 OGl THR A 409 2203 1613 1676 377 291 165 O

ATOM 754 CG2 THR A 409 3.675 45.014 -9.231 1.00 17.90 C

ANISOU 754 CG2 THR A 409 2609 2032 2160 383 331 145 C

ATOM 755 C THR A 409 2.173 45.279 -11.775 1.00 13.19 C

ANISOU 755 C THR A 409 1938 1568 1504 373 373 249 C

ATOM 756 O THR A 409 2.350 46.489 -11.845 1.00 14.45 O

ANISOU 756 O THR A 409 2086 1713 1691 385 414 281 O

ATOM 757 N ARG A 410 2.504 44.458 -12.760 1.00 12.02 N

ANISOU 757 N ARG A 410 1768 1468 1330 358 353 225 N

ATOM 758 CA ARG A 410 3.067 44.978 -13.996 1.00 17.41 C

ANISOU 758 CA ARG A 410 2415 2193 2008 356 379 238 C

ATOM 759 CB ARG A 410 3.540 43.839 -14.915 1.00 14.74 C

ANISOU 759 CB ARG A 410 2058 1903 1639 338 348 191 C

ATOM 760 CG ARG A 410 4.837 43.144 -14.477 1.00 14.07 C

ANISOU 760 CG ARG A 410 1989 1775 1583 329 318 110 C

ATOM 761 CD ARG A 410 6.033 44.088 -14.502 1.00 16.20 C ANISOU 761 CD ARG A 410 2252 2009 1893 336 347 98 C

ATOM 762 NE ARG A 410 6.355 44.545 -15.858 1.00 19.23 N

ANISOU 762 NE ARG A 410 2597 2450 2260 333 379 121 N

ATOM 763 CZ ARG A 410 6.312 45.809 -16.279 1.00 17.07 C

ANISOU 763 CZ ARG A 410 2304 2184 1999 346 428 179 C

ATOM 764 NHl ARG A 410 5.974 46.790 -15.459 1.00 20.77 N ANISOU 764 NHl ARG A 410 2787 2604 2502 361 452 215 N

ATOM 765 NH2 ARG A 410 6.615 46.093 -17.539 1.00 17.60 N ANISOU 765 NH2 ARG A 410 2335 2307 2045 343 455 200 N

ATOM 766 C ARG A 410 2.048 45.859 -14.717 1.00 13.30 C

ANISOU 766 C ARG A 410 1866 1718 1468 365 418 320 C

ATOM 767 0 ARG A 410 2.400 46.911 -15.231 1.00 12.87 O

ANISOU 767 O ARG A 410 1790 1668 1430 373 458 355 O

ATOM 768 N ALA A 411 0.791 45.416 -14.760 1.00 12.38 N

ANISOU 768 N ALA A 411 1749 1634 1320 363 405 353 N

ATOM 769 CA ALA A 411 -0.273 46.175 -15.419 1.00 13.24 C

ANISOU 769 CA ALA A 411 1830 1788 1411 372 437 433 C

ATOM 770 CB ALA A 411 -1.611 45.416 -15.321 1.00 9.21 C

ANISOU 770 CB ALA A 411 1322 1306 871 367 412 452 C

ATOM 771 C ALA A 411 -0.422 47.593 -14.861 1.00 20.13 C

ANISOU 771 C ALA A 411 2705 2614 2327 390 482 483 C

ATOM 772 O ALA A 411 -0.614 48.548 -15.610 1.00 20.23 O

ANISOU 772 O ALA A 411 2688 2655 2343 399 520 542 O

ATOM 773 N ILE A 412 -0.341 47.720 -13.543 1.00 17.32 N

ANISOU 773 N ILE A 412 2385 2189 2006 396 479 458 N

ATOM 774 CA ILE A 412 -0.492 49.008 -12.876 1.00 14.97 C

ANISOU 774 CA ILE A 412 2092 1842 1754 413 520 494 C

ATOM 775 CB ILE A 412 -0.796 48.805 -11.370 1.00 15.07 C

ANISOU 775 CB ILE A 412 2147 1795 1785 419 506 466 C

ATOM 776 CG2 ILE A 412 -0.631 50.104 -10.611 1.00 30.41 C

ANISOU 776 CG2 ILE A 412 4095 3679 3780 435 546 480 C

ATOM 777 CGI ILE A 412 -2.219 48.240 -11.173 1.00 9.30 C

ANISOU 777 CGI ILE A 412 1421 1087 1024 417 494 498 C

ATOM 778 CD1 ILE A 412 -2.368 47.409 -9.881 1.00 13.49 C

ANISOU 778 CD1 ILE A 412 1996 1577 1552 415 463 453 C

ATOM 779 C ILE A 412 0.762 49.866 -13.077 1.00 18.84 C

ANISOU 779 C ILE A 412 2569 2304 2286 419 547 479 C

ATOM 780 O ILE A 412 0.682 51.096 -13.152 1.00 19.34 O

ANISOU 780 O ILE A 412 2613 2348 2387 432 592 526 O

ATOM 781 N GLN A 413 1.915 49.217 -13.211 1.00 11.69 N

ANISOU 781 N GLN A 413 1670 1393 1379 408 522 415 N

ATOM 782 CA GLN A 413 3.171 49.930 -13.475 1.00 15.55 C

ANISOU 782 CA GLN A 413 2144 1856 1909 412 545 396 C

ATOM 783 CB GLN A 413 4.382 49.003 -13.304 1.00 19.58 C

ANISOU 783 CB GLN A 413 2670 2348 2420 399 507 312 C

ATOM 784 CG GLN A 413 4.682 48.582 -11.878 1.00 18.21 C ANISOU 784 CG GLN A 413 2541 2111 2268 401 474 253 C

ATOM 785 CD GLN A 413 5.964 47.747 -11.762 1.00 29.55 C

ANISOU 785 CD GLN A 413 3987 3527 3713 390 437 174 C

ATOM 786 OEl GLN A 413 6.318 46.992 -12.673 1.00 19.73 O

ANISOU 786 OEl GLN A 413 2726 2327 2443 377 421 155 O

ATOM 787 NE2 GLN A 413 6.655 47.873 -10.629 1.00 17.59 N

ANISOU 787 NE2 GLN A 413 2500 1947 2236 397 422 125 N

ATOM 788 C GLN A 413 3.163 50.515 -14.877 1.00 23.04 C

ANISOU 788 C GLN A 413 3047 2862 2844 413 581 453 C

ATOM 789 O GLN A 413 3.606 51.645 -15.099 1.00 19.53 O

ANISOU 789 O GLN A 413 2581 2396 2444 423 624 483 O

ATOM 790 N ILE A 414 2.638 49.741 -15.820 1.00 15.01 N

ANISOU 790 N ILE A 414 2016 1920 1769 402 563 468 N

ATOM 791 CA ILE A 414 2.548 50.167 -17.209 1.00 20.00 C

ANISOU 791 CA ILE A 414 2605 2620 2373 403 591 524 C

ATOM 792 CB ILE A 414 2.209 48.973 -18.127 1.00 23.71 C

ANISOU 792 CB ILE A 414 3066 3171 2773 388 556 508 C

ATOM 793 CG2 ILE A 414 1.805 49.461 -19.521 1.00 25.34 C

ANISOU 793 CG2 ILE A 414 3229 3459 2940 391 584 578 C

ATOM 794 CGI ILE A 414 3.402 48.001 -18.184 1.00 14.02 C

ANISOU 794 CGI ILE A 414 1849 1937 1542 372 525 420 C

ATOM 795 CD1 ILE A 414 3.081 46.654 -18.765 1.00 14.34 C

ANISOU 795 CD1 ILE A 414 1886 2039 1525 356 482 384 C

ATOM 796 C ILE A 414 1.507 51.275 -17.376 1.00 23.46 C

ANISOU 796 C ILE A 414 3023 3068 2823 419 631 616 C

ATOM 797 0 ILE A 414 1.722 52.228 -18.114 1.00 21.00 O

ANISOU 797 O ILE A 414 2678 2772 2527 428 674 670 O

ATOM 798 N ASN A 415 0.378 51.138 -16.688 1.00 15.91 N

ANISOU 798 N ASN A 415 2083 2100 1862 422 619 635 N

ATOM 799 CA ASN A 415 -0.683 52.141 -16.732 1.00 25.22 C

ANISOU 799 CA ASN A 415 3239 3279 3064 440 649 713 C

ATOM 800 CB ASN A 415 -1.773 51.700 -17.703 1.00 26.45 C

ANISOU 800 CB ASN A 415 3365 3514 3170 442 627 752 C

ATOM 801 CG ASN A 415 -2.859 52.732 -17.864 1.00 28.46 C

ANISOU 801 CG ASN A 415 3585 3774 3456 464 652 827 C

ATOM 802 OD1 ASN A 415 -2.817 53.798 -17.247 1.00 23.58 O ANISOU 802 OD1 ASN A 415 2964 3096 2898 479 688 849 O

ATOM 803 ND2 ASN A 415 -3.840 52.426 -18.707 1.00 34.53 N ANISOU 803 ND2 ASN A 415 4324 4613 4183 466 634 866 N

ATOM 804 C ASN A 415 -1.287 52.350 -15.347 1.00 25.60 C

ANISOU 804 C ASN A 415 3316 3260 3151 449 647 700 C

ATOM 805 O ASN A 415 -2.167 51.598 -14.945 1.00 16.32 O

ANISOU 805 O ASN A 415 2154 2095 1952 446 615 685 O

ATOM 806 N PRO A 416 -0.798 53.363 -14.611 1.00 23.28 N

ANISOU 806 N PRO A 416 3030 2898 2918 458 684 702 N

ATOM 807 CD PRO A 416 0.291 54.254 -15.044 1.00 19.76 C ANISOU 807 CD PRO A 416 2562 2432 2512 462 722 713 C

ATOM 808 CA PRO A 416 -1.215 53.636 -13.227 1.00 30.06 C

ANISOU 808 CA PRO A 416 3918 3691 3813 467 686 682 C

ATOM 809 CB PRO A 416 -0.288 54.784 -12.798 1.00 30.68 C

ANISOU 809 CB PRO A 416 3993 3705 3960 475 727 678 C

ATOM 810 CG PRO A 416 0.877 54.712 -13.746 1.00 26.18 C

ANISOU 810 CG PRO A 416 3402 3158 3387 469 728 661 C

ATOM 811 C PRO A 416 -2.680 54.064 -13.141 1.00 26.28 C

ANISOU 811 C PRO A 416 3414 3226 3346 483 696 729 C

ATOM 812 O PRO A 416 -3.257 54.081 -12.048 1.00 30.35 O

ANISOU 812 O PRO A 416 3951 3703 3877 488 695 710 O

ATOM 813 N ALA A 417 -3.271 54.360 -14.294 1.00 20.72 N

ANISOU 813 N ALA A 417 2664 2579 2629 491 704 789 N

ATOM 814 CA ALA A 417 -4.657 54.820 -14.387 1.00 19.92 C

ANISOU 814 CA ALA A 417 2533 2496 2542 506 714 843 C

ATOM 815 CB ALA A 417 -4.780 55.878 -15.474 1.00 21.56 C

ANISOU 815 CB ALA A 417 2687 2733 2771 521 750 922 C

ATOM 816 C ALA A 417 -5.601 53.674 -14.688 1.00 18.33 C

ANISOU 816 C ALA A 417 2331 2349 2284 497 670 837 C

ATOM 817 O ALA A 417 -6.768 53.891 -15.025 1.00 21.44 O

ANISOU 817 O ALA A 417 2694 2773 2679 507 673 886 O

ATOM 818 N PHE A 418 -5.091 52.450 -14.588 1.00 17.33 N

ANISOU 818 N PHE A 418 2236 2234 2113 478 630 779 N

ATOM 819 CA PHE A 418 -5.821 51.282 -15.066 1.00 18.14 C

ANISOU 819 CA PHE A 418 2336 2394 2163 466 588 771 C

ATOM 820 CB PHE A 418 -4.826 50.226 -15.575 1.00 22.47 C

ANISOU 820 CB PHE A 418 2902 2973 2663 444 557 723 C

ATOM 821 CG PHE A 418 -5.459 49.049 -16.295 1.00 26.17 C

ANISOU 821 CG PHE A 418 3360 3509 3076 430 516 716 C

ATOM 822 CD1 PHE A 418 -6.766 49.097 -16.741 1.00 22.97 C

ANISOU 822 CD 1 PHE A 418 2922 3145 2661 436 512 764 C

ATOM 823 CD2 PHE A 418 -4.718 47.902 -16.538 1.00 26.09 C

ANISOU 823 CD2 PHE A 418 3370 3520 3024 409 484 662 C

ATOM 824 CE1 PHE A 418 -7.327 48.019 -17.406 1.00 31.86 C

ANISOU 824 CE1 PHE A 418 4037 4333 3736 422 475 756 C

ATOM 825 CE2 PHE A 418 -5.272 46.826 -17.202 1.00 21.15 C

ANISOU 825 CE2 PHE A 418 2731 2955 2347 395 449 652 C

ATOM 826 CZ PHE A 418 -6.584 46.886 -17.635 1.00 23.84 C

ANISOU 826 CZ PHE A 418 3041 3337 2678 401 445 699 C

ATOM 827 C PHE A 418 -6.662 50.741 -13.922 1.00 14.98 C

ANISOU 827 C PHE A 418 1961 1960 1771 465 572 744 C

ATOM 828 O PHE A 418 -6.171 49.955 -13.109 1.00 17.48 O

ANISOU 828 O PHE A 418 2319 2245 2078 453 550 685 O

ATOM 829 N ALA A 419 -7.925 51.176 -13.879 1.00 15.87 N

ANISOU 829 N ALA A 419 2048 2082 1901 477 586 789 N

ATOM 830 CA ALA A 419 -8.851 50.897 -12.775 1.00 22.20 C ANISOU 830 CA ALA A 419 2868 2850 2719 480 583 774 C

ATOM 831 CB ALA A 419 -10.213 51.587 -13.045 1.00 22.95 C ANISOU 831 CB ALA A 419 2921 2963 2836 495 605 839 C

ATOM 832 C ALA A 419 -9.045 49.398 -12.546 1.00 24.04 C

ANISOU 832 C ALA A 419 3126 3098 2912 461 538 728 C

ATOM 833 O ALA A 419 -8.953 48.910 -11.410 1.00 19.30 O

ANISOU 833 O ALA A 419 2564 2453 2316 457 530 684 O

ATOM 834 N ASP A 420 -9.292 48.666 -13.629 1.00 17.75 N

ANISOU 834 N ASP A 420 2307 2364 2073 449 509 740 N

ATOM 835 CA ASP A 420 -9.476 47.211 -13.548 1.00 21.16 C

ANISOU 835 CA ASP A 420 2758 2813 2470 430 466 700 C

ATOM 836 CB ASP A 420 -9.707 46.610 -14.935 1.00 28.16 C

ANISOU 836 CB ASP A 420 3612 3779 3309 418 441 719 C

ATOM 837 CG ASP A 420 -11.046 46.998 -15.523 1.00 40.81 C ANISOU 837 CG ASP A 420 5172 5423 4913 427 448 781 C

ATOM 838 OD1 ASP A 420 -11.809 47.723 -14.849 1.00 35.03 O ANISOU 838 OD1 ASP A 420 4433 4654 4221 442 475 810 O

ATOM 839 OD2 ASP A 420 -11.333 46.572 -16.661 1.00 41.60 O ANISOU 839 OD2 ASP A 420 5244 5594 4969 419 428 801 O

ATOM 840 C ASP A 420 -8.329 46.466 -12.850 1.00 12.55 C

ANISOU 840 C ASP A 420 1714 1685 1371 418 446 634 C

ATOM 841 O ASP A 420 -8.564 45.558 -12.040 1.00 10.35 O

ANISOU 841 O ASP A 420 1462 1381 1089 410 425 600 O

ATOM 842 N ALA A 421 -7.093 46.841 -13.160 1.00 11.43 N

ANISOU 842 N ALA A 421 1580 1537 1227 417 454 619 N ATOM 843 CA ALA A 421 -5.950 46.124 -12.615 1.00 16.79 C ANISOU 843 CA ALA A 421 2300 2184 1896 404 433 559 C ATOM 844 CB ALA A 421 -4.657 46.524 -13.331 1.00 11.82 C ANISOU 844 CB ALA A 421 1667 1567 1258 400 443 552 C

ATOM 845 C ALA A 421 -5.832 46.319 -11.112 1.00 21.30 C

ANISOU 845 C ALA A 421 2910 2684 2497 412 442 532 C

ATOM 846 O ALA A 421 -5.397 45.409 -10.393 1.00 13.06 O

ANISOU 846 O ALA A 421 1904 1615 1445 402 414 487 O

ATOM 847 N HIS A 422 -6.200 47.504 -10.635 1.00 18.62 N

ANISOU 847 N HIS A 422 2564 2317 2195 430 481 561 N

ATOM 848 CA HIS A 422 -6.191 47.771 -9.198 1.00 23.53 C

ANISOU 848 CA HIS A 422 3221 2879 2839 438 494 536 C

ATOM 849 CB HIS A 422 -6.458 49.252 -8.913 1.00 20.81 C

ANISOU 849 CB HIS A 422 2861 2509 2537 457 544 570 C

ATOM 850 CG HIS A 422 -5.294 50.145 -9.211 1.00 18.91 C

ANISOU 850 CG HIS A 422 2618 2250 2319 461 566 571 C

ATOM 851 CD2 HIS A 422 -5.024 50.939 -10.275 1.00 15.10 C ANISOU 851 CD2 HIS A 422 2098 1790 1850 466 589 612 C

ATOM 852 ND1 HIS A 422 -4.229 50.284 -8.351 1.00 17.65 N ANISOU 852 ND1 HIS A 422 2497 2039 2171 459 567 528 N

ATOM 853 CE1 HIS A 422 -3.360 51.138 -8.861 1.00 11.53 C ANISOU 853 CE1 HIS A 422 1708 1252 1422 463 591 541 C

ATOM 854 NE2 HIS A 422 -3.817 51.546 -10.030 1.00 15.54 N

ANISOU 854 NE2 HIS A 422 2169 1805 1930 466 607 593 N

ATOM 855 C HIS A 422 -7.233 46.913 -8.485 1.00 15.29 C

ANISOU 855 C HIS A 422 2190 1833 1786 435 477 527 C

ATOM 856 O HIS A 422 -7.000 46.398 -7.393 1.00 15.46 O

ANISOU 856 O HIS A 422 2251 1820 1803 432 465 489 O

ATOM 857 N SER A 423 -8.388 46.785 -9.114 1.00 9.16 N

ANISOU 857 N SER A 423 1378 1095 1006 435 477 566 N

ATOM 858 CA SER A 423 -9.501 45.988 -8.595 1.00 11.03 C

ANISOU 858 CA SER A 423 1619 1334 1237 432 464 567 C

ATOM 859 CB SER A 423 -10.732 46.211 -9.506 1.00 14.09 C

ANISOU 859 CB SER A 423 1958 1766 1628 435 472 622 C

ATOM 860 OG SER A 423 -11.904 45.630 -8.969 1.00 16.66 O

ANISOU 860 OG SER A 423 2284 2089 1958 434 468 630 O

ATOM 861 C SER A 423 -9.124 44.505 -8.553 1.00 12.70 C

ANISOU 861 C SER A 423 1854 1552 1420 413 419 527 C

ATOM 862 0 SER A 423 -9.417 43.795 -7.591 1.00 12.55 O

ANISOU 862 O SER A 423 1862 1506 1400 410 408 505 O

ATOM 863 N ASN A 424 -8.468 44.036 -9.607 1.00 9.14 N

ANISOU 863 N ASN A 424 1391 1137 945 400 394 519 N

ATOM 864 CA ASN A 424 -7.983 42.666 -9.653 1.00 10.25 C

ANISOU 864 CA ASN A 424 1552 1282 1061 382 351 480 C

ATOM 865 CB ASN A 424 -7.428 42.337 -11.048 1.00 16.68 C

ANISOU 865 CB ASN A 424 2342 2151 1844 370 332 480 C

ATOM 866 CG ASN A 424 -8.511 42.308 -12.110 1.00 25.94 C

ANISOU 866 CG ASN A 424 3471 3386 3001 367 332 522 C

ATOM 867 OD1 ASN A 424 -9.673 42.025 -11.815 1.00 23.74 O ANISOU 867 OD1 ASN A 424 3181 3106 2731 369 331 542 O

ATOM 868 ND2 ASN A 424 -8.141 42.601 -13.345 1.00 15.55 N ANISOU 868 ND2 ASN A 424 2126 2123 1658 364 333 536 N

ATOM 869 C ASN A 424 -6.919 42.441 -8.590 1.00 10.12 C

ANISOU 869 C ASN A 424 1583 1213 1050 382 342 434 C

ATOM 870 O ASN A 424 -6.918 41.414 -7.905 1.00 10.43 O

ANISOU 870 O ASN A 424 1647 1231 1084 375 315 407 O

ATOM 871 N LEU A 425 -6.033 43.413 -8.415 1.00 9.49 N

ANISOU 871 N LEU A 425 1513 1109 982 392 363 427 N

ATOM 872 CA LEU A 425 -5.027 43.296 -7.350 1.00 15.15 C

ANISOU 872 CA LEU A 425 2275 1775 1705 393 353 384 C

ATOM 873 CB LEU A 425 -4.023 44.428 -7.407 1.00 12.13 C

ANISOU 873 CB LEU A 425 1897 1371 1339 402 377 381 C

ATOM 874 CG LEU A 425 -2.885 44.383 -6.380 1.00 20.00 C

ANISOU 874 CG LEU A 425 2939 2315 2346 406 362 335 C

ATOM 875 CD1 LEU A 425 -2.119 43.081 -6.487 1.00 17.34 C ANISOU 875 CD 1 LEU A 425 2617 1976 1996 393 311 292 C

ATOM 876 CD2 LEU A 425 -1.966 45.565 -6.630 1.00 18.20 C ANISOU 876 CD2 LEU A 425 2705 2066 2145 415 388 337 C

ATOM 877 C LEU A 425 -5.686 43.299 -5.988 1.00 18.93 C

ANISOU 877 C LEU A 425 2781 2221 2193 402 364 379 C

ATOM 878 O LEU A 425 -5.283 42.558 -5.091 1.00 10.05 O

ANISOU 878 O LEU A 425 1691 1067 1059 399 339 345 O

ATOM 879 N ALA A 426 -6.686 44.159 -5.827 1.00 7.87 N

ANISOU 879 N ALA A 426 1361 823 807 414 401 414 N

ATOM 880 CA ALA A 426 -7.465 44.188 -4.588 1.00 15.17 C

ANISOU 880 CA ALA A 426 2307 1722 1736 423 418 415 C

ATOM 881 CB ALA A 426 -8.575 45.224 -4.679 1.00 10.53 C

ANISOU 881 CB ALA A 426 1689 1143 1171 436 461 460 C

ATOM 882 C ALA A 426 -8.062 42.817 -4.320 1.00 21.35 C

ANISOU 882 C ALA A 426 3098 2512 2504 412 387 408 C

ATOM 883 O ALA A 426 -8.059 42.336 -3.182 1.00 14.50 O

ANISOU 883 O ALA A 426 2265 1616 1628 413 380 388 O

ATOM 884 N SER A 427 -8.586 42.186 -5.366 1.00 13.52 N

ANISOU 884 N SER A 427 2073 1558 1508 401 369 426 N

ATOM 885 CA SER A 427 -9.158 40.845 -5.203 1.00 14.70 C

ANISOU 885 CA SER A 427 2225 1712 1649 389 340 422 C

ATOM 886 CB SER A 427 -9.826 40.379 -6.495 1.00 27.53 C

ANISOU 886 CB SER A 427 3807 3384 3269 378 326 448 C

ATOM 887 OG SER A 427 -10.744 41.356 -6.951 1.00 43.04 O

ANISOU 887 OG SER A 427 5737 5370 5246 388 359 491 O

ATOM 888 C SER A 427 -8.156 39.784 -4.684 1.00 15.54 C

ANISOU 888 C SER A 427 2368 1794 1744 379 301 378 C

ATOM 889 O SER A 427 -8.541 38.890 -3.917 1.00 18.60 O

ANISOU 889 O SER A 427 2773 2164 2131 375 287 372 O

ATOM 890 N ILE A 428 -6.887 39.887 -5.089 1.00 15.46 N

ANISOU 890 N ILE A 428 2367 1779 1727 375 284 351 N

ATOM 891 CA ILE A 428 -5.835 38.989 -4.594 1.00 12.77 C

ANISOU 891 CA ILE A 428 2059 1411 1382 369 245 310 C

ATOM 892 CB ILE A 428 -4.461 39.178 -5.320 1.00 9.36 C

ANISOU 892 CB ILE A 428 1628 979 949 366 226 285 C

ATOM 893 CG2 ILE A 428 -3.425 38.216 -4.724 1.00 17.36 C

ANISOU 893 CG2 ILE A 428 2672 1956 1967 363 182 240 C

ATOM 894 CGI ILE A 428 -4.583 38.883 -6.802 1.00 19.91 C

ANISOU 894 CGI ILE A 428 2926 2364 2275 355 216 297 C

ATOM 895 CD1 ILE A 428 -4.951 37.439 -7.105 1.00 32.67 C

ANISOU 895 CD 1 ILE A 428 4526 3997 3891 339 179 278 C

ATOM 896 C ILE A 428 -5.606 39.237 -3.118 1.00 10.66 C

ANISOU 896 C ILE A 428 1833 1104 1113 380 254 293 C

ATOM 897 O ILE A 428 -5.441 38.295 -2.321 1.00 15.14 O

ANISOU 897 O ILE A 428 2426 1650 1676 377 227 275 O

ATOM 898 N HIS A 429 -5.580 40.508 -2.739 1.00 15.32 N

ANISOU 898 N HIS A 429 2429 1685 1706 394 291 301 N

ATOM 899 CA HIS A 429 -5.387 40.841 -1.330 1.00 18.04 C ANISOU 899 CA HIS A 429 2815 1996 2043 405 301 287 C

ATOM 900 CB HIS A 429 -5.203 42.358 -1.127 1.00 12.12 C

ANISOU 900 CB HIS A 429 2067 1235 1303 420 341 294 C

ATOM 901 CG HIS A 429 -3.912 42.897 -1.683 1.00 14.61 C

ANISOU 901 CG HIS A 429 2380 1542 1629 419 332 271 C

ATOM 902 CD2 HIS A 429 -3.653 43.977 -2.461 1.00 28.37 C

ANISOU 902 CD2 HIS A 429 4098 3292 3392 423 360 286 C

ATOM 903 NDl HIS A 429 -2.692 42.301 -1.446 1.00 29.78 N

ANISOU 903 NDl HIS A 429 4325 3444 3547 414 291 228 N

ATOM 904 CE1 HIS A 429 -1.738 42.986 -2.054 1.00 28.64 C

ANISOU 904 CE1 HIS A 429 4168 3294 3422 414 295 213 C

ATOM 905 NE2 HIS A 429 -2.293 44.009 -2.678 1.00 15.62 N

ANISOU 905 NE2 HIS A 429 2491 1660 1786 420 337 250 N

ATOM 906 C HIS A 429 -6.577 40.289 -0.538 1.00 20.06 C

ANISOU 906 C HIS A 429 3078 2250 2293 408 311 307 C

ATOM 907 O HIS A 429 -6.408 39.605 0.486 1.00 19.73 O

ANISOU 907 O HIS A 429 3071 2188 2237 410 292 293 O

ATOM 908 N LYS A 430 -7.778 40.547 -1.042 1.00 14.94 N

ANISOU 908 N LYS A 430 2396 1625 1657 409 338 344 N

ATOM 909 CA LYS A 430 -9.001 40.048 -0.400 1.00 13.00 C

ANISOU 909 CA LYS A 430 2151 1378 1411 412 351 368 C

ATOM 910 CB LYS A 430 -10.243 40.437 -1.217 1.00 13.06 C

ANISOU 910 CB LYS A 430 2113 1414 1438 412 377 409 C

ATOM 911 CG LYS A 430 -11.583 40.074 -0.544 1.00 26.39 C

ANISOU 911 CG LYS A 430 3798 3097 3131 417 397 437 C

ATOM 912 CD LYS A 430 -12.765 40.643 -1.320 1.00 24.93 C

ANISOU 912 CD LYS A 430 3566 2936 2968 421 424 479 C

ATOM 913 CE LYS A 430 -14.064 40.612 -0.510 1.00 20.68 C

ANISOU 913 CE LYS A 430 3029 2387 2440 430 454 508 C

ATOM 914 NZ LYS A 430 -14.609 39.239 -0.226 1.00 10.76 N

ANISOU 914 NZ LYS A 430 1776 1129 1185 419 433 514 N

ATOM 915 C LYS A 430 -8.944 38.536 -0.215 1.00 17.26 C

ANISOU 915 C LYS A 430 2700 1913 1945 399 311 357 C

ATOM 916 0 LYS A 430 -9.112 38.020 0.898 1.00 20.07 O

ANISOU 916 O LYS A 430 3087 2249 2292 403 309 356 O

ATOM 917 N ASP A 431 -8.704 37.828 -1.305 1.00 15.73 N

ANISOU 917 N ASP A 431 2480 1739 1758 383 280 352 N

ATOM 918 CA ASP A 431 -8.770 36.370 -1.293 1.00 15.14 C

ANISOU 918 CA ASP A 431 2405 1658 1687 370 243 346 C

ATOM 919 CB ASP A 431 -8.693 35.804 -2.717 1.00 21.88 C

ANISOU 919 CB ASP A 431 3223 2539 2551 355 216 346 C

ATOM 920 CG ASP A 431 -9.976 36.019 -3.497 1.00 46.93 C

ANISOU 920 CG ASP A 431 6356 5745 5732 353 237 386 C

ATOM 921 OD1 ASP A 431 -11.043 36.158 -2.862 1.00 43.19 O

ANISOU 921 OD1 ASP A 431 5879 5265 5265 360 264 413 O

ATOM 922 OD2 ASP A 431 -9.918 36.045 -4.745 1.00 62.15 O ANISOU 922 OD2 ASP A 431 8253 7705 7657 345 225 391 O

ATOM 923 C ASP A 431 -7.674 35.794 -0.422 1.00 31.69 C

ANISOU 923 C ASP A 431 4542 3723 3774 371 212 312 C

ATOM 924 0 ASP A 431 -7.766 34.661 0.048 1.00 39.27 O

ANISOU 924 O ASP A 431 5512 4669 4740 365 188 311 O

ATOM 925 N SER A 432 -6.644 36.596 -0.191 1.00 30.17 N

ANISOU 925 N SER A 432 4371 3520 3571 378 214 287 N ATOM 926 CA SER A 432 -5.548 36.202 0.677 1.00 35.78 C ANISOU 926 CA SER A 432 5122 4202 4272 382 183 255 C

ATOM 927 CB SER A 432 -4.240 36.801 0.159 1.00 37.88 C ANISOU 927 CB SER A 432 5389 4463 4540 382 168 222 C ATOM 928 OG SER A 432 -3.945 36.289 -1.127 1.00 29.88 O ANISOU 928 OG SER A 432 4343 3466 3543 369 145 214 O

ATOM 929 C SER A 432 -5.790 36.629 2.126 1.00 40.24 C

ANISOU 929 C SER A 432 5726 4747 4816 398 205 262 C

ATOM 930 O SER A 432 -4.930 36.436 2.984 1.00 35.17 O

ANISOU 930 O SER A 432 5121 4082 4161 405 181 239 O

ATOM 931 N GLY A 433 -6.955 37.218 2.391 1.00 25.74 N

ANISOU 931 N GLY A 433 3882 2919 2978 407 249 294 N ATOM 932 CA GLY A 433 -7.318 37.626 3.742 1.00 36.20 C ANISOU 932 CA GLY A 433 5245 4227 4283 425 274 305 C

ATOM 933 C GLY A 433 -6.844 39.006 4.185 1.00 39.63 C

ANISOU 933 C GLY A 433 5703 4650 4706 441 299 293 C

ATOM 934 O GLY A 433 -7.233 39.480 5.251 1.00 51.07 O

ANISOU 934 O GLY A 433 7182 6085 6137 457 325 304 O

ATOM 935 N ASN A 434 -6.010 39.650 3.371 1.00 22.79 N

ANISOU 935 N ASN A 434 3554 2521 2583 436 293 273 N ATOM 936 CA ASN A 434 -5.460 40.968 3.689 1.00 23.42 C ANISOU 936 CA ASN A 434 3650 2586 2661 450 316 261 C ATOM 937 CB ASN A 434 -4.144 41.165 2.936 1.00 30.75 C ANISOU 937 CB ASN A 434 4570 3513 3602 442 288 228 C ATOM 938 CG ASN A 434 -3.426 42.425 3.339 1.00 19.51 C ANISOU 938 CG ASN A 434 3162 2068 2182 455 305 211 C ATOM 939 OD1 ASN A 434 -4.014 43.332 3.934 1.00 24.19 O ANISOU 939 OD1 ASN A 434 3766 2651 2774 469 344 227 O ATOM 940 ND2 ASN A 434 -2.144 42.506 2.995 1.00 22.94 N ANISOU 940 ND2 ASN A 434 3594 2493 2628 449 276 174 N

ATOM 941 C ASN A 434 -6.431 42.089 3.336 1.00 29.64 C

ANISOU 941 C ASN A 434 4412 3386 3466 457 369 292 C

ATOM 942 0 ASN A 434 -6.244 42.811 2.357 1.00 13.64 O

ANISOU 942 O ASN A 434 2352 1370 1460 453 383 296 O

ATOM 943 N ILE A 435 -7.467 42.240 4.150 1.00 32.51 N

ANISOU 943 N ILE A 435 4787 3744 3821 468 401 317 N

ATOM 944 CA ILE A 435 -8.578 43.106 3.796 1.00 12.04 C

ANISOU 944 CA ILE A 435 2163 1162 1250 474 449 351 C

ATOM 945 CB ILE A 435 -9.777 42.934 4.767 1.00 14.08 C ANISOU 945 CB ILE A 435 2437 1413 1500 485 478 378 C

ATOM 946 CG2 ILE A 435 -10.944 43.824 4.343 1.00 21.77 C

ANISOU 946 CG2 ILE A 435 3373 2397 2503 492 526 414 C

ATOM 947 CGI ILE A 435 -10.198 41.471 4.864 1.00 11.44 C

ANISOU 947 CGI ILE A 435 2101 1088 1157 475 450 385 C

ATOM 948 CD1 ILE A 435 -10.579 40.819 3.567 1.00 19.89 C

ANISOU 948 CD 1 ILE A 435 3122 2185 2250 457 432 396 C

ATOM 949 C ILE A 435 -8.263 44.592 3.674 1.00 10.00 C

ANISOU 949 C ILE A 435 1899 891 1008 484 483 351 C

ATOM 950 O ILE A 435 -8.793 45.251 2.788 1.00 19.75 O

ANISOU 950 O ILE A 435 3091 2142 2272 483 509 376 O

ATOM 951 N PRO A 436 -7.438 45.144 4.592 1.00 21.66 N

ANISOU 951 N PRO A 436 3418 2339 2472 495 482 326 N

ATOM 952 CD PRO A 436 -6.948 44.550 5.849 1.00 23.74 C

ANISOU 952 CD PRO A 436 3738 2582 2700 504 456 304 C

ATOM 953 CA PRO A 436 -7.090 46.569 4.496 1.00 25.00 C

ANISOU 953 CA PRO A 436 3834 2744 2919 504 515 325 C

ATOM 954 CB PRO A 436 -6.187 46.798 5.715 1.00 24.69 C

ANISOU 954 CB PRO A 436 3850 2670 2862 517 499 289 C

ATOM 955 CG PRO A 436 -6.646 45.768 6.695 1.00 25.89 C

ANISOU 955 CG PRO A 436 4040 2822 2974 523 483 293 C

ATOM 956 C PRO A 436 -6.357 46.942 3.208 1.00 5.69 C

ANISOU 956 C PRO A 436 1348 311 501 493 506 320 C

ATOM 957 0 PRO A 436 -6.622 48.001 2.692 1.00 12.55 O

ANISOU 957 O PRO A 436 2186 1179 1402 496 544 341 O

ATOM 958 N GLU A 437 -5.445 46.106 2.723 1.00 20.57 N

ANISOU 958 N GLU A 437 3234 2205 2376 480 460 293 N

ATOM 959 CA GLU A 437 -4.811 46.371 1.440 1.00 18.83 C

ANISOU 959 CA GLU A 437 2975 1998 2179 469 454 292 C

ATOM 960 CB GLU A 437 -3.581 45.481 1.224 1.00 24.47 C

ANISOU 960 CB GLU A 437 3703 2712 2884 458 401 252 C

ATOM 961 CG GLU A 437 -2.400 45.807 2.147 1.00 47.93 C

ANISOU 961 CG GLU A 437 6708 5650 5853 464 381 206 C

ATOM 962 CD GLU A 437 -1.611 47.049 1.743 1.00 41.92 C

ANISOU 962 CD GLU A 437 5925 4874 5129 466 402 192 C

ATOM 963 OEl GLU A 437 -0.429 47.152 2.149 1.00 28.88 O ANISOU 963 OEl GLU A 437 4286 3205 3483 464 375 146 O

ATOM 964 OE2 GLU A 437 -2.158 47.920 1.027 1.00 42.10 O ANISOU 964 OE2 GLU A 437 5914 4904 5178 468 444 228 O

ATOM 965 C GLU A 437 -5.821 46.159 0.318 1.00 16.70 C

ANISOU 965 C GLU A 437 2658 1765 1920 463 468 332 C

ATOM 966 O GLU A 437 -5.788 46.860 -0.692 1.00 18.49 O

ANISOU 966 O GLU A 437 2848 2006 2173 462 487 352 O

ATOM 967 N ALA A 438 -6.730 45.206 0.505 1.00 19.34 N

ANISOU 967 N ALA A 438 2994 2116 2240 459 457 344 N

ATOM 968 CA ALA A 438 -7.825 45.015 -0.446 1.00 13.99 C ANISOU 968 CA ALA A 438 2270 1471 1575 454 468 381 C

ATOM 969 CB ALA A 438 -8.646 43.811 -0.064 1.00 11.82 C

ANISOU 969 CB ALA A 438 2001 1204 1285 449 450 386 C

ATOM 970 C ALA A 438 -8.696 46.259 -0.504 1.00 27.57 C

ANISOU 970 C ALA A 438 3964 3190 3322 468 519 418 C

ATOM 971 O ALA A 438 -8.993 46.773 -1.572 1.00 12.41 O

ANISOU 971 O ALA A 438 2000 1291 1423 468 533 446 O

ATOM 972 N ILE A 439 -9.095 46.752 0.660 1.00 18.27 N

ANISOU 972 N ILE A 439 2814 1985 2142 481 547 419 N

ATOM 973 CA ILE A 439 -9.835 47.996 0.730 1.00 27.92 C

ANISOU 973 CA ILE A 439 4017 3198 3395 495 598 451 C

ATOM 974 CB ILE A 439 -10.231 48.334 2.183 1.00 22.56 C

ANISOU 974 CB ILE A 439 3379 2487 2706 508 626 447 C

ATOM 975 CG2 ILE A 439 -10.735 49.771 2.300 1.00 17.70 C

ANISOU 975 CG2 ILE A 439 2745 1852 2127 522 681 474 C

ATOM 976 CGI ILE A 439 -11.306 47.361 2.664 1.00 12.64 C

ANISOU 976 CGI ILE A 439 2129 1240 1432 508 621 460 C

ATOM 977 CD1 ILE A 439 -11.412 47.304 4.214 1.00 7.96 C

ANISOU 977 CD 1 ILE A 439 1593 619 814 520 634 447 C

ATOM 978 C ILE A 439 -9.081 49.158 0.074 1.00 21.42 C

ANISOU 978 C ILE A 439 3171 2367 2600 498 618 455 C

ATOM 979 O ILE A 439 -9.688 49.951 -0.611 1.00 14.55 O

ANISOU 979 O ILE A 439 2258 1507 1762 504 648 493 O

ATOM 980 N ALA A 440 -7.761 49.223 0.237 1.00 15.61 N

ANISOU 980 N ALA A 440 2461 1614 1857 493 598 419 N

ATOM 981 CA ALA A 440 -6.987 50.323 -0.342 1.00 14.41 C

ANISOU 981 CA ALA A 440 2287 1448 1738 495 618 423 C

ATOM 982 CB ALA A 440 -5.560 50.302 0.189 1.00 21.45 C

ANISOU 982 CB ALA A 440 3216 2311 2624 492 592 373 C

ATOM 983 C ALA A 440 -6.990 50.327 -1.866 1.00 10.86 C

ANISOU 983 C ALA A 440 1788 1035 1304 489 613 452 C

ATOM 984 O ALA A 440 -7.190 51.369 -2.512 1.00 11.81 O

ANISOU 984 O ALA A 440 1870 1156 1461 497 648 487 O

ATOM 985 N SER A 441 -6.755 49.154 -2.438 1.00 10.68 N

ANISOU 985 N SER A 441 1765 1040 1253 476 570 438 N

ATOM 986 CA SER A 441 -6.729 48.997 -3.886 1.00 19.60 C

ANISOU 986 CA SER A 441 2853 2209 2387 470 559 462 C

ATOM 987 CB SER A 441 -6.129 47.640 -4.259 1.00 11.03 C

ANISOU 987 CB SER A 441 1780 1141 1268 454 507 431 C

ATOM 988 OG SER A 441 -4.718 47.632 -4.028 1.00 22.71 O

ANISOU 988 OG SER A 441 3288 2594 2747 449 490 391 O

ATOM 989 C SER A 441 -8.105 49.205 -4.552 1.00 13.53 C

ANISOU 989 C SER A 441 2038 1471 1630 476 578 514 C

ATOM 990 O SER A 441 -8.168 49.791 -5.619 1.00 14.39 O

ANISOU 990 O SER A 441 2107 1604 1757 479 591 549 O

ATOM 991 N TYR A 442 -9.196 48.728 -3.938 1.00 8.95 N ANISOU 991 N TYR A 442 1465 894 1043 478 579 521 N

ATOM 992 CA TYR A 442 -10.543 49.010 -4.472 1.00 15.87 C

ANISOU 992 CA TYR A 442 2298 1795 1937 485 598 571 C

ATOM 993 CB TYR A 442 -11.646 48.294 -3.683 1.00 22.42 C

ANISOU 993 CB TYR A 442 3140 2620 2757 485 596 573 C

ATOM 994 CG TYR A 442 -11.767 46.834 -3.995 1.00 13.97 C

ANISOU 994 CG TYR A 442 2074 1575 1658 468 551 557 C

ATOM 995 CD1 TYR A 442 -11.882 46.392 -5.299 1.00 12.56 C ANISOU 995 CD 1 TYR A 442 1859 1440 1474 458 526 576 C

ATOM 996 CE1 TYR A 442 -11.991 45.034 -5.587 1.00 14.69 C

ANISOU 996 CE1 TYR A 442 2131 1729 1720 442 486 561 C

ATOM 997 CD2 TYR A 442 -11.752 45.890 -2.970 1.00 14.23 C ANISOU 997 CD2 TYR A 442 2148 1590 1671 463 534 527 C

ATOM 998 CE2 TYR A 442 -11.851 44.556 -3.234 1.00 13.50 C

ANISOU 998 CE2 TYR A 442 2056 1515 1560 448 495 515 C

ATOM 999 CZ TYR A 442 -11.965 44.123 -4.541 1.00 11.99 C

ANISOU 999 CZ TYR A 442 1828 1363 1365 436 471 530 C

ATOM 1000 OH TYR A 442 -12.042 42.776 -4.791 1.00 15.29 O ANISOU 1000 OH TYR A 442 2248 1795 1767 420 433 517 O

ATOM 1001 C TYR A 442 -10.871 50.492 -4.489 1.00 14.61 C

ANISOU 1001 C TYR A 442 2113 1618 1819 501 648 608 C

ATOM 1002 O TYR A 442 -11.449 50.992 -5.454 1.00 16.07 O

ANISOU 1002 O TYR A 442 2252 1830 2024 507 660 655 O

ATOM 1003 N ARG A 443 -10.511 51.199 -3.421 1.00 13.00 N

ANISOU 1003 N ARG A 443 1940 1371 1629 509 677 589 N

ATOM 1004 CA ARG A 443 -10.732 52.654 -3.367 1.00 7.63 C

ANISOU 1004 CA ARG A 443 1236 666 996 524 728 622 C

ATOM 1005 CB ARG A 443 -10.322 53.204 -1.991 1.00 18.54 C ANISOU 1005 CB ARG A 443 2662 1997 2385 529 753 590 C

ATOM 1006 CG ARG A 443 -11.323 52.949 -0.872 1.00 29.56 C ANISOU 1006 CG ARG A 443 4084 3378 3770 535 767 588 C

ATOM 1007 CD ARG A 443 -10.779 53.502 0.441 1.00 36.72 C ANISOU 1007 CD ARG A 443 5038 4236 4677 540 789 555 C

ATOM 1008 NE ARG A 443 -11.432 52.949 1.622 1.00 39.76 N ANISOU 1008 NE ARG A 443 5464 4611 5034 544 791 542 N

ATOM 1009 CZ ARG A 443 -12.688 53.201 1.945 1.00 29.46 C ANISOU 1009 CZ ARG A 443 4147 3302 3745 553 824 573 C ATOM 1010 NHl ARG A 443 -13.411 53.991 1.162 1.00 55.55 N ANISOU 1010 NHl ARG A 443 7397 6614 7096 560 854 619 N ATOM 1011 NH2 ARG A 443 -13.221 52.679 3.039 1.00 32.09 N ANISOU 1011 NH2 ARG A 443 4519 3624 4050 557 827 562 N

ATOM 1012 C ARG A 443 -9.943 53.353 -4.468 1.00 12.49 C

ANISOU 1012 C ARG A 443 1819 1292 1635 525 734 642 C

ATOM 1013 O ARG A 443 -10.440 54.277 -5.115 1.00 18.86 O

ANISOU 1013 O ARG A 443 2581 2104 2479 535 764 692 O

ATOM 1014 N THR A 444 -8.707 52.915 -4.700 1.00 30.27 N ANISOU 1014 N THR A 444 4091 3544 3866 514 706 606 N

ATOM 1015 CA THR A 444 -7.933 53.467 -5.811 1.00 22.50 C

ANISOU 1015 CA THR A 444 3077 2573 2901 513 711 627 C

ATOM 1016 CB THR A 444 -6.492 52.906 -5.867 1.00 18.22 C

ANISOU 1016 CB THR A 444 2564 2022 2335 500 679 579 C

ATOM 1017 OGl THR A 444 -5.745 53.344 -4.721 1.00 10.25 O

ANISOU 1017 OGl THR A 444 1593 960 1342 502 691 539 O

ATOM 1018 CG2 THR A 444 -5.771 53.371 -7.125 1.00 18.35 C

ANISOU 1018 CG2 THR A 444 2546 2058 2368 500 686 606 C

ATOM 1019 C THR A 444 -8.682 53.208 -7.136 1.00 15.65 C

ANISOU 1019 C THR A 444 2161 1762 2025 514 698 676 C

ATOM 1020 O THR A 444 -8.844 54.107 -7.939 1.00 16.70 O

ANISOU 1020 O THR A 444 2252 1906 2188 524 724 725 O

ATOM 1021 N ALA A 445 -9.161 51.985 -7.343 1.00 15.44 N

ANISOU 1021 N ALA A 445 2140 1769 1957 503 658 664 N

ATOM 1022 CA ALA A 445 -9.917 51.660 -8.560 1.00 15.28 C

ANISOU 1022 CA ALA A 445 2077 1806 1924 501 642 708 C

ATOM 1023 CB ALA A 445 -10.447 50.223 -8.511 1.00 13.39 C

ANISOU 1023 CB ALA A 445 1851 1592 1645 487 600 685 C

ATOM 1024 C ALA A 445 -11.081 52.614 -8.756 1.00 16.49 C

ANISOU 1024 C ALA A 445 2189 1963 2113 518 678 768 C

ATOM 1025 O ALA A 445 -11.318 53.100 -9.856 1.00 19.73 O

ANISOU 1025 O ALA A 445 2556 2409 2532 523 685 820 O

ATOM 1026 N LEU A 446 -11.822 52.827 -7.675 1.00 17.52 N

ANISOU 1026 N LEU A 446 2334 2059 2262 525 700 764 N

ATOM 1027 CA LEU A 446 -13.000 53.665 -7.669 1.00 17.84 C

ANISOU 1027 CA LEU A 446 2339 2096 2341 540 735 817 C

ATOM 1028 CB LEU A 446 -13.828 53.373 -6.410 1.00 12.63 C

ANISOU 1028 CB LEU A 446 1708 1407 1684 542 746 798 C

ATOM 1029 CG LEU A 446 -14.552 52.012 -6.411 1.00 16.07 C

ANISOU 1029 CG LEU A 446 2151 1872 2083 530 708 786 C

ATOM 1030 CDl LEU A 446 -14.949 51.584 -5.003 1.00 18.99 C

ANISOU 1030 CDl LEU A 446 2564 2206 2447 530 717 753 C

ATOM 1031 CD2 LEU A 446 -15.777 52.053 -7.346 1.00 19.59 C

ANISOU 1031 CD2 LEU A 446 2546 2358 2540 534 706 846 C

ATOM 1032 C LEU A 446 -12.636 55.158 -7.773 1.00 24.24 C

ANISOU 1032 C LEU A 446 3127 2878 3205 555 782 849 C

ATOM 1033 O LEU A 446 -13.440 55.966 -8.226 1.00 20.46 O

ANISOU 1033 O LEU A 446 2605 2407 2763 568 809 908 O

ATOM 1034 N LYS A 447 -11.424 55.511 -7.355 1.00 24.56 N

ANISOU 1034 N LYS A 447 3195 2884 3253 553 792 813 N

ATOM 1035 CA LYS A 447 -10.905 56.863 -7.564 1.00 24.37 C

ANISOU 1035 CA LYS A 447 3146 2830 3282 564 835 841 C

ATOM 1036 CB LYS A 447 -9.553 57.041 -6.844 1.00 18.97 C

ANISOU 1036 CB LYS A 447 2503 2101 2604 557 841 787 C

ATOM 1037 CG LYS A 447 -9.107 58.497 -6.740 1.00 44.56 C ANISOU 1037 CG LYS A 447 5722 5295 5913 567 894 809 C

ATOM 1038 CD LYS A 447 -7.935 58.668 -5.789 1.00 49.94 C ANISOU 1038 CD LYS A 447 6447 5924 6604 559 899 749 C

ATOM 1039 CE LYS A 447 -7.553 60.139 -5.658 1.00 67.00 C

ANISOU 1039 CE LYS A 447 8581 8031 8844 568 953 770 C

ATOM 1040 NZ LYS A 447 -6.415 60.355 -4.718 1.00 69.42 N

ANISOU 1040 NZ LYS A 447 8926 8282 9167 561 953 706 N

ATOM 1041 C LYS A 447 -10.758 57.079 -9.074 1.00 22.08 C

ANISOU 1041 C LYS A 447 2810 2587 2993 567 828 894 C

ATOM 1042 O LYS A 447 -11.258 58.058 -9.632 1.00 23.31 O

ANISOU 1042 O LYS A 447 2919 2746 3191 581 860 957 O

ATOM 1043 N LEU A 448 -10.086 56.130 -9.720 1.00 23.46 N

ANISOU 1043 N LEU A 448 2997 2800 3118 553 786 870 N

ATOM 1044 CA LEU A 448 -9.888 56.105 -11.173 1.00 22.94 C ANISOU 1044 CA LEU A 448 2893 2789 3034 552 772 913 C

ATOM 1045 CB LEU A 448 -8.968 54.935 -11.538 1.00 13.07 C ANISOU 1045 CB LEU A 448 1672 1567 1727 533 727 864 C

ATOM 1046 CG LEU A 448 -7.513 55.141 -11.126 1.00 21.47 C ANISOU 1046 CG LEU A 448 2767 2588 2803 528 735 819 C ATOM 1047 CDl LEU A 448 -6.700 53.841 -11.178 1.00 17.60 C ANISOU 1047 CDl LEU A 448 2313 2115 2258 508 688 761 C ATOM 1048 CD2 LEU A 448 -6.911 56.200 -12.023 1.00 14.86 C ANISOU 1048 CD2 LEU A 448 1893 1755 1999 537 768 867 C

ATOM 1049 C LEU A 448 -11.170 55.986 -11.988 1.00 26.03 C

ANISOU 1049 C LEU A 448 3242 3233 3413 558 762 972 C

ATOM 1050 O LEU A 448 -11.311 56.623 -13.030 1.00 21.99 O

ANISOU 1050 O LEU A 448 2686 2755 2912 567 775 1035 O

ATOM 1051 N LYS A 449 -12.094 55.145 -11.529 1.00 19.12 N

ANISOU 1051 N LYS A 449 2381 2369 2516 551 739 955 N ATOM 1052 C A LYS A 449 -13.324 54.885 -12.267 1.00 27.14 C ANISOU 1052 CA LYS A 449 3359 3435 3517 553 725 1006 C ATOM 1053 CB LYS A 449 -13.195 53.592 -13.077 1.00 26.43 C

ANISOU 1053 CB LYS A 449 3273 3406 3363 534 674 986 C ATOM 1054 CG LYS A 449 -14.374 53.340 -14.013 1.00 29.69 C ANISOU 1054 CG LYS A 449 3644 3880 3757 534 657 1042 C ATOM 1055 CD LYS A 449 -13.987 52.413 -15.152 1.00 26.82 C ANISOU 1055 CD LYS A 449 3274 3585 3331 518 615 1036 C

ATOM 1056 CE LYS A 449 -14.046 50.953 -14.757 1.00 20.60 C

ANISOU 1056 CE LYS A 449 2520 2801 2505 497 574 975 C ATOM 1057 NZ LYS A 449 -13.270 50.095 -15.724 1.00 16.31 N

ANISOU 1057 NZ LYS A 449 1980 2313 1905 480 538 952 N

ATOM 1058 C LYS A 449 -14.512 54.796 -11.307 1.00 25.07 C

ANISOU 1058 C LYS A 449 3103 3146 3276 557 736 1004 C

ATOM 1059 O LYS A 449 -14.844 53.705 -10.821 1.00 20.32 O

ANISOU 1059 O LYS A 449 2529 2549 2645 545 708 965 O

ATOM 1060 N PRO A 450 -15.139 55.951 -11.021 1.00 25.24 N ANISOU 1060 N PRO A 450 3098 3138 3354 575 781 1049 N

ATOM 1061 CD PRO A 450 -14.750 57.239 -11.630 1.00 38.72 C

ANISOU 1061 CD PRO A 450 4769 4839 5104 590 817 1102 C

ATOM 1062 CA PRO A 450 -16.238 56.109 -10.063 1.00 20.29 C

ANISOU 1062 CA PRO A 450 2474 2477 2756 582 803 1053 C

ATOM 1063 CB PRO A 450 -16.732 57.535 -10.335 1.00 31.04 C

ANISOU 1063 CB PRO A 450 3790 3824 4182 601 851 1122 C

ATOM 1064 CG PRO A 450 -15.526 58.253 -10.835 1.00 37.83 C

ANISOU 1064 CG PRO A 450 4642 4675 5055 605 865 1128 C

ATOM 1065 C PRO A 450 -17.376 55.124 -10.308 1.00 20.47 C

ANISOU 1065 C PRO A 450 2487 2541 2751 573 772 1065 C

ATOM 1066 O PRO A 450 -17.960 54.617 -9.357 1.00 18.25 O

ANISOU 1066 O PRO A 450 2231 2235 2469 570 773 1037 O

ATOM 1067 N ASP A 451 -17.685 54.884 -11.577 1.00 19.72 N

ANISOU 1067 N ASP A 451 2355 2506 2631 570 747 1109 N

ATOM 1068 CA ASP A 451 -18.715 53.938 -11.971 1.00 16.73 C

ANISOU 1068 CA ASP A 451 1962 2170 2224 560 714 1124 C

ATOM 1069 CB ASP A 451 -19.461 54.466 -13.202 1.00 22.59 C

ANISOU 1069 CB ASP A 451 2645 2965 2971 567 714 1206 C

ATOM 1070 CG ASP A 451 -20.818 53.842 -13.374 1.00 27.70 C

ANISOU 1070 CG ASP A 451 3272 3641 3612 561 696 1233 C

ATOM 1071 ODl ASP A 451 -20.983 52.642 -13.054 1.00 33.00 O ANISOU 1071 ODl ASP A 451 3970 4318 4251 545 665 1188 O

ATOM 1072 OD2 ASP A 451 -21.731 54.555 -13.837 1.00 50.80 O ANISOU 1072 OD2 ASP A 451 6152 6581 6568 573 713 1303 O

ATOM 1073 C ASP A 451 -18.093 52.569 -12.259 1.00 14.96 C

ANISOU 1073 C ASP A 451 1766 1978 1939 538 665 1071 C

ATOM 1074 O ASP A 451 -17.658 52.286 -13.375 1.00 15.17 O

ANISOU 1074 O ASP A 451 1777 2058 1928 530 638 1084 O

ATOM 1075 N PHE A 452 -18.043 51.725 -11.235 1.00 16.98 N

ANISOU 1075 N PHE A 452 2065 2201 2185 528 654 1013 N

ATOM 1076 CA PHE A 452 -17.329 50.455 -11.328 1.00 17.87 C

ANISOU 1076 CA PHE A 452 2209 2331 2249 508 611 958 C

ATOM 1077 CB PHE A 452 -15.863 50.677 -10.942 1.00 16.96 C

ANISOU 1077 CB PHE A 452 2129 2185 2128 508 615 910 C

ATOM 1078 CG PHE A 452 -14.936 49.562 -11.346 1.00 14.68 C

ANISOU 1078 CG PHE A 452 1864 1920 1793 488 573 864 C

ATOM 1079 CDl PHE A 452 -15.421 48.376 -11.863 1.00 19.05 C ANISOU 1079 CDl PHE A 452 2412 2516 2312 472 534 858 C

ATOM 1080 CD2 PHE A 452 -13.578 49.722 -11.223 1.00 13.14 C ANISOU 1080 CD2 PHE A 452 1696 1706 1591 486 573 826 C

ATOM 1081 CE1 PHE A 452 -14.558 47.361 -12.235 1.00 15.63 C ANISOU 1081 CE1 PHE A 452 1998 2103 1838 454 497 815 C

ATOM 1082 CE2 PHE A 452 -12.702 48.712 -11.594 1.00 25.12 C ANISOU 1082 CE2 PHE A 452 3234 3244 3069 468 535 784 C

ATOM 1083 CZ PHE A 452 -13.197 47.528 -12.102 1.00 24.31 C ANISOU 1083 CZ PHE A 452 3124 3182 2932 452 497 778 C

ATOM 1084 C PHE A 452 -17.979 49.428 -10.400 1.00 21.32 C

ANISOU 1084 C PHE A 452 2674 2747 2681 499 598 925 C

ATOM 1085 O PHE A 452 -17.509 49.200 -9.292 1.00 17.68 O

ANISOU 1085 O PHE A 452 2255 2240 2222 498 605 877 O

ATOM 1086 N PRO A 453 -19.072 48.806 -10.859 1.00 18.12 N

ANISOU 1086 N PRO A 453 2243 2374 2268 492 579 954 N

ATOM 1087 CD PRO A 453 -19.695 49.007 -12.178 1.00 20.78 C ANISOU 1087 CD PRO A 453 2529 2771 2594 492 567 1013 C

ATOM 1088 CA PRO A 453 -19.861 47.911 -10.022 1.00 25.57 C

ANISOU 1088 CA PRO A 453 3205 3296 3215 484 573 935 C

ATOM 1089 CB PRO A 453 -20.852 47.310 -11.012 1.00 25.73 C

ANISOU 1089 CB PRO A 453 3186 3368 3221 475 546 975 C

ATOM 1090 CG PRO A 453 -21.057 48.390 -12.005 1.00 22.67 C ANISOU 1090 CG PRO A 453 2755 3017 2843 487 559 1034 C

ATOM 1091 C PRO A 453 -19.035 46.813 -9.345 1.00 21.48 C

ANISOU 1091 C PRO A 453 2736 2757 2671 470 548 868 C

ATOM 1092 O PRO A 453 -19.215 46.612 -8.147 1.00 19.94 O

ANISOU 1092 O PRO A 453 2571 2517 2488 473 563 844 O

ATOM 1093 N ASP A 454 -18.169 46.118 -10.077 1.00 23.48 N

ANISOU 1093 N ASP A 454 2995 3041 2887 455 511 842 N

ATOM 1094 CA ASP A 454 -17.403 45.035 -9.459 1.00 27.11 C

ANISOU 1094 CA ASP A 454 3497 3478 3324 441 486 783 C

ATOM 1095 CB ASP A 454 -16.432 44.398 -10.439 1.00 29.66 C

ANISOU 1095 CB ASP A 454 3820 3839 3609 425 448 760 C

ATOM 1096 CG ASP A 454 -17.126 43.539 -11.454 1.00 28.73 C

ANISOU 1096 CG ASP A 454 3674 3776 3467 411 416 781 C ATOM 1097 ODl ASP A 454 -18.350 43.326 -11.315 1.00 32.12 O ANISOU 1097 ODl ASP A 454 4085 4207 3913 411 419 811 O ATOM 1098 OD2 ASP A 454 -16.444 43.076 -12.383 1.00 31.45 O ANISOU 1098 OD2 ASP A 454 4013 4162 3775 399 387 767 O

ATOM 1099 C ASP A 454 -16.634 45.521 -8.255 1.00 17.52 C

ANISOU 1099 C ASP A 454 2324 2209 2122 451 510 747 C

ATOM 1100 O ASP A 454 -16.672 44.903 -7.193 1.00 23.74 O

ANISOU 1100 O ASP A 454 3147 2963 2910 448 509 717 O

ATOM 1101 N ALA A 455 -15.929 46.630 -8.426 1.00 11.38 N

ANISOU 1101 N ALA A 455 1543 1424 1355 462 532 753 N

ATOM 1102 CA ALA A 455 -15.089 47.142 -7.366 1.00 11.72 C ANISOU 1102 CA ALA A 455 1627 1419 1408 470 554 717 C

ATOM 1103 CB ALA A 455 -14.174 48.222 -7.894 1.00 15.72 C

ANISOU 1103 CB ALA A 455 2123 1926 1924 479 571 726 C

ATOM 1104 C ALA A 455 -15.946 47.679 -6.211 1.00 15.10 C

ANISOU 1104 C ALA A 455 2066 1809 1865 485 593 729 C

ATOM 1105 O ALA A 455 -15.642 47.437 -5.051 1.00 12.46 O

ANISOU 1105 O ALA A 455 1774 1438 1524 485 599 693 O

ATOM 1106 N TYR A 456 -17.016 48.401 -6.520 1.00 13.79 N ANISOU 1106 N TYR A 456 1860 1651 1726 496 619 781 N

ATOM 1107 CA TYR A 456 -17.847 48.936 -5.439 1.00 17.86 C ANISOU 1107 CA TYR A 456 2386 2130 2271 510 659 792 C

ATOM 1108 CB TYR A 456 -18.998 49.788 -5.975 1.00 14.34 C ANISOU 1108 CB TYR A 456 1890 1696 1862 522 687 855 C

ATOM 1109 CG TYR A 456 -19.747 50.489 -4.869 1.00 15.25 C ANISOU 1109 CG TYR A 456 2014 1769 2011 537 734 867 C ATOM 1110 CDl TYR A 456 -19.337 51.733 -4.402 1.00 22.31 C ANISOU 1110 CDl TYR A 456 2914 2628 2934 552 776 869 C

ATOM 1111 CEl TYR A 456 -20.021 52.368 -3.367 1.00 20.35 C ANISOU 1111 CEl TYR A 456 2677 2340 2716 565 821 878 C ATOM 1112 CD2 TYR A 456 -20.838 49.892 -4.262 1.00 17.01 C ANISOU 1112 CD2 TYR A 456 2241 1983 2239 537 740 875 C

ATOM 1113 CE2 TYR A 456 -21.520 50.516 -3.242 1.00 21.46 C ANISOU 1113 CE2 TYR A 456 2815 2508 2832 550 786 885 C

ATOM 1114 CZ TYR A 456 -21.110 51.754 -2.803 1.00 19.66 C

ANISOU 1114 CZ TYR A 456 2593 2247 2629 564 827 886 C

ATOM 1115 OH TYR A 456 -21.791 52.363 -1.773 1.00 20.98 O ANISOU 1115 OH TYR A 456 2772 2374 2824 577 874 894 O

ATOM 1116 C TYR A 456 -18.403 47.808 -4.573 1.00 18.40 C

ANISOU 1116 C TYR A 456 2481 2185 2324 502 647 770 C

ATOM 1117 O TYR A 456 -18.357 47.864 -3.339 1.00 15.84 O

ANISOU 1117 0 TYR A 456 2195 1823 2000 508 669 747 O

ATOM 1118 N CYS A 457 -18.954 46.788 -5.225 1.00 14.24 N

ANISOU 1118 N CYS A 457 2265 1670 1477 787 451 365 N

ATOM 1119 CA CYS A 457 -19.583 45.680 -4.503 1.00 16.52 C ANISOU 1119 CA CYS A 457 2573 1944 1758 765 403 342 C

ATOM 1120 CB CYS A 457 -20.423 44.825 -5.454 1.00 17.71 C

ANISOU 1120 CB CYS A 457 2745 2112 1872 780 362 344 C

ATOM 1121 SG CYS A 457 -21.866 45.706 -6.100 1.00 21.63 S

ANISOU 1121 SG CYS A 457 3227 2620 2372 780 374 388 S

ATOM 1122 C CYS A 457 -18.571 44.812 -3.760 1.00 16.85 C

ANISOU 1122 C CYS A 457 2628 1972 1802 757 383 306 C

ATOM 1123 O CYS A 457 -18.852 44.321 -2.656 1.00 14.20 O

ANISOU 1123 0 CYS A 457 2300 1616 1479 727 359 290 O

ATOM 1124 N ASN A 458 -17.401 44.611 -4.357 1.00 16.34 N

ANISOU 1124 N ASN A 458 2565 1920 1723 784 392 296 N

ATOM 1125 CA ASN A 458 -16.354 43.857 -3.679 1.00 9.19 C

ANISOU 1125 CA ASN A 458 1669 1002 823 779 375 264 C

ATOM 1126 CB ASN A 458 -15.243 43.424 -4.655 1.00 9.42 C

ANISOU 1126 CB ASN A 458 1703 1052 826 820 379 255 C

ATOM 1127 CG ASN A 458 -15.633 42.196 -5.473 1.00 22.55 C ANISOU 1127 CG ASN A 458 3398 2726 2443 845 333 236 C ATOM 1128 OD1 ASN A 458 -16.383 41.345 -5.002 1.00 26.12 O ANISOU 1128 ODl ASN A 458 3872 3164 2889 824 287 221 O ATOM 1129 ND2 ASN A 458 -15.137 42.108 -6.703 1.00 16.00 N ANISOU 1129 ND2 ASN A 458 2575 1923 1581 888 345 240 N

ATOM 1130 C ASN A 458 -15.820 44.627 -2.494 1.00 12.53 C

ANISOU 1130 C ASN A 458 2073 1401 1289 750 402 266 C

ATOM 1131 O ASN A 458 -15.548 44.054 -1.428 1.00 12.71 O

ANISOU 1131 0 ASN A 458 2105 1402 1324 725 380 242 O

ATOM 1132 N LEU A 459 -15.696 45.936 -2.658 1.00 15.96 N

ANISOU 1132 N LEU A 459 2483 1838 1744 752 448 294 N

ATOM 1133 CA LEU A 459 -15.324 46.807 -1.542 1.00 12.17 C

ANISOU 1133 CA LEU A 459 1989 1331 1304 723 473 298 C

ATOM 1134 CB LEU A 459 -15.108 48.255 -2.031 1.00 10.18 C

ANISOU 1134 CB LEU A 459 1712 1085 1071 733 522 333 C

ATOM 1135 CG LEU A 459 -15.047 49.332 -0.944 1.00 14.53 C

ANISOU 1135 CG LEU A 459 2253 1606 1663 703 546 342 C

ATOM 1136 CDl LEU A 459 -13.920 49.082 0.058 1.00 6.02 C

ANISOU 1136 CDl LEU A 459 1178 504 606 683 538 321 C

ATOM 1137 CD2 LEU A 459 -14.935 50.719 -1.569 1.00 18.81 C ANISOU 1137 CD2 LEU A 459 2773 2154 2222 715 589 378 C

ATOM 1138 C LEU A 459 -16.391 46.748 -0.435 1.00 19.67 C

ANISOU 1138 C LEU A 459 2948 2258 2266 689 458 292 C

ATOM 1139 0 LEU A 459 -16.075 46.644 0.750 1.00 13.98 O

ANISOU 1139 0 LEU A 459 2234 1513 1567 661 450 276 O

ATOM 1140 N ALA A 460 -17.659 46.798 -0.822 1.00 5.92 N

ANISOU 1140 N ALA A 460 1209 527 513 691 452 307 N

ATOM 1141 CA ALA A 460 -18.736 46.701 0.156 1.00 10.78 C ANISOU 1141 CA ALA A 460 1831 1127 1139 662 439 306 C

ATOM 1142 CB ALA A 460 -20.092 46.750 -0.541 1.00 11.56 C

ANISOU 1142 CB ALA A 460 1927 1243 1223 670 433 329 C

ATOM 1143 C ALA A 460 -18.612 45.417 0.990 1.00 13.43 C

ANISOU 1143 C ALA A 460 2187 1450 1466 641 394 274 C

ATOM 1144 0 ALA A 460 -18.807 45.426 2.210 1.00 14.25 O

ANISOU 1144 0 ALA A 460 2295 1531 1587 611 390 265 O

ATOM 1145 N HIS A 461 -18.280 44.311 0.335 1.00 13.15 N

ANISOU 1145 N HIS A 461 2166 1428 1404 657 358 257 N

ATOM 1146 CA HIS A 461 -18.120 43.065 1.065 1.00 10.92 C

ANISOU 1146 CA HIS A 461 1903 1131 1113 639 312 228 C

ATOM 1147 CB HIS A 461 -18.032 41.852 0.135 1.00 12.42 C

ANISOU 1147 CB HIS A 461 2113 1337 1268 662 269 212 C

ATOM 1148 CG HIS A 461 -18.170 40.550 0.854 1.00 18.67 C

ANISOU 1148 CG HIS A 461 2927 2114 2052 640 214 186 C

ATOM 1149 CD2 HIS A 461 -19.170 40.070 1.634 1.00 18.54 C

ANISOU 1149 CD2 HIS A 461 2918 2087 2038 609 184 187 C

ATOM 1150 ND1 HIS A 461 -17.179 39.593 0.869 1.00 18.48 N

ANISOU 1150 ND1 HIS A 461 2920 2085 2018 650 185 156 N

ATOM 1151 CE1 HIS A 461 -17.570 38.570 1.611 1.00 21.33 C

ANISOU 1151 CE1 HIS A 461 3299 2431 2376 624 136 139 C

ATOM 1152 NE2 HIS A 461 -18.776 38.836 2.086 1.00 10.74 N ANISOU 1152 NE2 HIS A 461 1952 1087 1042 598 135 159 N

ATOM 1153 C HIS A 461 -16.925 43.125 2.025 1.00 15.98 C

ANISOU 1153 C HIS A 461 2544 1750 1777 623 319 208 C

ATOM 1154 0 HIS A 461 -17.021 42.659 3.157 1.00 10.60 O

ANISOU 1154 0 HIS A 461 1873 1049 1106 592 298 192 O

ATOM 1155 N CYS A 462 -15.809 43.708 1.592 1.00 11.11 N

ANISOU 1155 N CYS A 462 1914 1138 1169 642 350 211 N

ATOM 1156 CA CYS A 462 -14.676 43.907 2.504 1.00 10.78 C

ANISOU 1156 CA CYS A 462 1868 1074 1154 625 358 198 C

ATOM 1157 CB CYS A 462 -13.508 44.619 1.798 1.00 12.28 C

ANISOU 1157 CB CYS A 462 2037 1274 1353 650 393 212 C

ATOM 1158 SG CYS A 462 -12.691 43.697 0.455 1.00 17.49 S

ANISOU 1158 SG CYS A 462 2700 1964 1981 696 380 202 S

ATOM 1159 C CYS A 462 -15.075 44.729 3.731 1.00 12.08 C

ANISOU 1159 C CYS A 462 2031 1213 1347 590 376 205 C

ATOM 1160 O CYS A 462 -14.657 44.440 4.866 1.00 11.32 O

ANISOU 1160 O CYS A 462 1945 1092 1265 562 361 186 O

ATOM 1161 N LEU A 463 -15.839 45.793 3.505 1.00 11.56 N

ANISOU 1161 N LEU A 463 1954 1151 1288 593 410 231 N

ATOM 1162 C A LEU A 463 -16.271 46.629 4.616 1.00 10.38 C

ANISOU 1162 CA LEU A 463 1805 976 1162 566 430 237 C

ATOM 1163 CB LEU A 463 -17.006 47.873 4.121 1.00 10.87 C

ANISOU 1163 CB LEU A 463 1852 1045 1232 578 470 268 C

ATOM 1164 CG LEU A 463 -16.124 48.754 3.238 1.00 7.67 C

ANISOU 1164 CG LEU A 463 1428 648 837 601 501 286 C

ATOM 1165 CDl LEU A 463 -16.947 49.908 2.664 1.00 8.70 C

ANISOU 1165 CDl LEU A 463 1545 787 975 615 536 318 C

ATOM 1166 CD2 LEU A 463 -14.919 49.278 4.003 1.00 15.61 C ANISOU 1166 CD2 LEU A 463 2433 1627 1871 585 513 280 C

ATOM 1167 C LEU A 463 -17.159 45.831 5.549 1.00 9.20 C

ANISOU 1167 C LEU A 463 1673 817 1004 539 399 222 C

ATOM 1168 0 LEU A 463 -17.098 46.005 6.758 1.00 13.92 O

ANISOU 1168 0 LEU A 463 2282 1391 1617 512 400 212 O

ATOM 1169 N GLN A 464 -17.958 44.929 4.979 1.00 12.87 N

ANISOU 1169 N GLN A 464 2143 1303 1445 548 369 222 N

ATOM 1170 CA GLN A 464 -18.819 44.059 5.782 1.00 14.38 C ANISOU 1170 CA GLN A 464 2347 1488 1627 522 335 213 C

ATOM 1171 CB GLN A 464 -19.770 43.250 4.891 1.00 15.98 C ANISOU 1171 CB GLN A 464 2552 1715 1804 535 303 222 C

ATOM 1172 CG GLN A 464 -20.860 42.491 5.659 1.00 16.96 C ANISOU 1172 CG GLN A 464 2684 1837 1923 508 271 223 C

ATOM 1173 CD GLN A 464 -22.059 43.362 6.000 1.00 12.97 C ANISOU 1173 CD GLN A 464 2165 1336 1429 501 302 251 C ATOM 1174 OEl GLN A 464 -22.266 44.421 5.403 1.00 14.21 O ANISOU 1174 OEl GLN A 464 2306 1500 1594 521 342 273 O ATOM 1175 NE2 GLN A 464 -22.867 42.908 6.958 1.00 14.56 N ANISOU 1175 NE2 GLN A 464 2370 1532 1631 473 285 254 N

ATOM 1176 C GLN A 464 -18.002 43.127 6.676 1.00 10.24 C

ANISOU 1176 C GLN A 464 1840 945 1104 500 300 182 C

ATOM 1177 0 GLN A 464 -18.293 42.964 7.865 1.00 11.99 O

ANISOU 1177 0 GLN A 464 2073 1150 1334 469 291 174 O

ATOM 1178 N ILE A 465 -16.970 42.530 6.096 1.00 9.07 N

ANISOU 1178 N ILE A 465 1696 802 950 516 282 166 N

ATOM 1179 CA ILE A 465 -16.114 41.571 6.802 1.00 10.01 C

ANISOU 1179 CA ILE A 465 1830 904 1070 499 246 137 C

ATOM 1180 CB ILE A 465 -14.998 41.034 5.861 1.00 12.67 C

ANISOU 1180 CB ILE A 465 2166 1252 1398 529 234 125 C

ATOM 1181 CG2 ILE A 465 -13.872 40.375 6.655 1.00 6.09 C

ANISOU 1181 CG2 ILE A 465 1341 397 576 513 209 99 C

ATOM 1182 CGI ILE A 465 -15.586 40.081 4.820 1.00 11.93 C

ANISOU 1182 CGI ILE A 465 2081 1180 1271 553 201 122 C

ATOM 1183 CD1 ILE A 465 -14.690 39.847 3.571 1.00 13.51 C

ANISOU 1183 CD 1 ILE A 465 2279 1399 1456 597 205 117 C

ATOM 1184 C ILE A 465 -15.466 42.188 8.039 1.00 11.71 C

ANISOU 1184 C ILE A 465 2047 1090 1312 471 263 131 C

ATOM 1185 O ILE A 465 -15.287 41.512 9.050 1.00 13.62 O

ANISOU 1185 0 ILE A 465 2305 1313 1557 442 234 112 O

ATOM 1186 N VAL A 466 -15.105 43.466 7.965 1.00 8.33 N

ANISOU 1186 N VAL A 466 1606 656 904 477 309 147 N

ATOM 1187 CA VAL A 466 -14.413 44.097 9.095 1.00 13.81 C

ANISOU 1187 CA VAL A 466 2306 1319 1623 451 322 141 C

ATOM 1188 CB VAL A 466 -13.136 44.845 8.652 1.00 15.22 C

ANISOU 1188 CB VAL A 466 2468 1492 1822 466 346 149 C

ATOM 1189 CGI VAL A 466 -12.236 43.892 7.871 1.00 9.24 C

ANISOU 1189 CGI VAL A 466 1705 752 1055 487 322 137 C

ATOM 1190 CG2 VAL A 466 -13.496 46.079 7.821 1.00 10.54 C

ANISOU 1190 CG2 VAL A 466 1857 914 1234 489 391 178 C

ATOM 1191 C VAL A 466 -15.304 45.014 9.929 1.00 15.87 C

ANISOU 1191 C VAL A 466 2573 1566 1893 433 349 152 C

ATOM 1192 0 VAL A 466 -14.816 45.731 10.808 1.00 14.11 O

ANISOU 1192 0 VAL A 466 2358 1315 1689 414 364 150 O

ATOM 1193 N CYS A 467 -16.606 44.972 9.656 1.00 8.09 N

ANISOU 1193 N CYS A 467 1584 598 892 439 353 166 N

ATOM 1194 CA CYS A 467 -17.574 45.789 10.375 1.00 13.33 C

ANISOU 1194 CA CYS A 467 2251 1252 1561 428 381 179 C

ATOM 1195 CB CYS A 467 -17.704 45.337 11.836 1.00 14.40 C

ANISOU 1195 CB CYS A 467 2411 1366 1696 392 362 161 C

ATOM 1196 SG CYS A 467 -18.326 43.632 12.036 1.00 15.10 S

ANISOU 1196 SG CYS A 467 2507 1469 1761 376 306 148 S

ATOM 1197 C CYS A 467 -17.254 47.278 10.291 1.00 15.67 C

ANISOU 1197 C CYS A 467 2541 1535 1879 438 427 194 C

ATOM 1198 O CYS A 467 -17.347 47.991 11.280 1.00 7.94 O ANISOU 1198 0 CYS A 467 1575 530 911 422 446 192 O

ATOM 1199 N ASP A 468 -16.871 47.730 9.099 1.00 11.66 N

ANISOU 1199 N ASP A 468 2013 1043 1374 466 444 209 N

ATOM 1200 CA ASP A 468 -16.737 49.160 8.824 1.00 10.75 C

ANISOU 1200 CA ASP A 468 1887 918 1277 479 487 230 C

ATOM 1201 CB ASP A 468 -15.660 49.401 7.754 1.00 5.26 C

ANISOU 1201 CB ASP A 468 1174 235 590 500 494 240 C

ATOM 1202 CG ASP A 468 -15.467 50.890 7.428 1.00 12.60 C

ANISOU 1202 CG ASP A 468 2092 1155 1542 511 535 265 C

ATOM 1203 OD1 ASP A 468 -16.448 51.660 7.471 1.00 21.68 O

ANISOU 1203 OD1 ASP A 468 3241 2303 2694 516 559 280 O

ATOM 1204 OD2 ASP A 468 -14.327 51.267 7.121 1.00 24.06 O

ANISOU 1204 OD2 ASP A 468 3533 2602 3009 514 541 271 O

ATOM 1205 C ASP A 468 -18.083 49.601 8.304 1.00 16.84 C

ANISOU 1205 C ASP A 468 2648 1709 2041 496 508 253 C

ATOM 1206 O ASP A 468 -18.471 49.207 7.207 1.00 12.30 O

ANISOU 1206 O ASP A 468 2059 1164 1451 517 501 264 O

ATOM 1207 N TRP A 469 -18.807 50.392 9.096 1.00 7.92 N

ANISOU 1207 N TRP A 469 1527 562 920 488 533 260 N

ATOM 1208 CA TRP A 469 -20.146 50.813 8.717 1.00 9.80 C

ANISOU 1208 CA TRP A 469 1753 817 1153 503 554 283 C

ATOM 1209 CB TRP A 469 -21.155 50.458 9.822 1.00 9.83 C

ANISOU 1209 CB TRP A 469 1770 815 1148 486 550 277 C

ATOM 1210 CG TRP A 469 -21.147 48.964 10.161 1.00 9.91 C

ANISOU 1210 CG TRP A 469 1789 836 1141 466 504 258 C

ATOM 1211 CD2 TRP A 469 -21.319 48.382 11.451 1.00 8.85 C

ANISOU 1211 CD2 TRP A 469 1675 688 1000 438 487 241 C

ATOM 1212 CE2 TRP A 469 -21.244 46.973 11.293 1.00 13.37 C

ANISOU 1212 CE2 TRP A 469 2249 1275 1557 426 439 229 C

ATOM 1213 CE3 TRP A 469 -21.535 48.908 12.732 1.00 12.32 C

ANISOU 1213 CE3 TRP A 469 2134 1102 1444 422 506 234 C

ATOM 1214 CD1 TRP A 469 -20.986 47.924 9.285 1.00 11.29 C

ANISOU 1214 CD1 TRP A 469 1955 1033 1300 472 469 255 C

ATOM 1215 NE1 TRP A 469 -21.035 46.716 9.961 1.00 10.26 N

ANISOU 1215 NE1 TRP A 469 1839 903 1157 449 429 236 N

ATOM 1216 CZ2 TRP A 469 -21.371 46.094 12.365 1.00 12.09 C

ANISOU 1216 CZ2 TRP A 469 2104 1104 1385 397 411 212 C

ATOM 1217 CZ3 TRP A 469 -21.656 48.022 13.803 1.00 13.18 C

ANISOU 1217 CZ3 TRP A 469 2261 1205 1541 393 480 217 C

ATOM 1218 CH2 TRP A 469 -21.579 46.637 13.609 1.00 11.32 C

ANISOU 1218 CH2 TRP A 469 2024 986 1293 380 432 208 C

ATOM 1219 C TRP A 469 -20.226 52.312 8.380 1.00 16.10 C

ANISOU 1219 C TRP A 469 2541 1605 1970 521 597 305 C

ATOM 1220 O TRP A 469 -21.266 52.933 8.560 1.00 14.95 O

ANISOU 1220 O TRP A 469 2393 1459 1828 529 621 321 O

ATOM 1221 N THR A 470 -19.133 52.887 7.891 1.00 20.10 N ANISOU 1221 N THR A 470 3042 2103 2491 527 606 309 N

ATOM 1222 CA THR A 470 -19.163 54.276 7.417 1.00 16.55 C

ANISOU 1222 CA THR A 470 2582 1645 2061 544 642 333 C

ATOM 1223 CB THR A 470 -17.795 54.729 6.894 1.00 20.69 C

ANISOU 1223 CB THR A 470 3098 2161 2601 547 645 339 C

ATOM 1224 OGl THR A 470 -16.785 54.463 7.876 1.00 19.56 O

ANISOU 1224 OGl THR A 470 2974 1991 2467 521 627 315 O

ATOM 1225 CG2 THR A 470 -17.800 56.234 6.560 1.00 19.57 C

ANISOU 1225 CG2 THR A 470 2948 2005 2482 559 679 365 C

ATOM 1226 C THR A 470 -20.191 54.435 6.291 1.00 19.62 C

ANISOU 1226 C THR A 470 2948 2065 2441 570 655 361 C

ATOM 1227 O THR A 470 -20.169 53.689 5.304 1.00 13.76 O

ANISOU 1227 O THR A 470 2193 1354 1682 582 637 365 O

ATOM 1228 N ASP A 471 -21.113 55.382 6.462 1.00 15.63 N

ANISOU 1228 N ASP A 471 2440 1551 1946 579 684 378 N

ATOM 1229 CA ASP A 471 -22.093 55.706 5.427 1.00 20.32 C

ANISOU 1229 CA ASP A 471 3012 2172 2537 603 699 408 C

ATOM 1230 CB ASP A 471 -21.404 56.344 4.211 1.00 21.65 C

ANISOU 1230 CB ASP A 471 3163 2351 2714 621 710 428 C

ATOM 1231 CG ASP A 471 -20.742 57.671 4.539 1.00 41.37 C

ANISOU 1231 CG ASP A 471 5665 4814 5238 620 736 436 C

ATOM 1232 OD1 ASP A 471 -21.109 58.285 5.561 1.00 47.65 O

ANISOU 1232 OD1 ASP A 471 6478 5580 6046 612 751 429 O

ATOM 1233 OD2 ASP A 471 -19.854 58.101 3.770 1.00 59.25 O

ANISOU 1233 OD2 ASP A 471 7918 7083 7511 627 741 449 O

ATOM 1234 C ASP A 471 -22.856 54.462 4.988 1.00 24.40 C

ANISOU 1234 C ASP A 471 3522 2722 3029 605 670 408 C

ATOM 1235 0 ASP A 471 -23.104 54.276 3.796 1.00 18.04 O

ANISOU 1235 0 ASP A 471 2698 1943 2213 622 664 426 O

ATOM 1236 N TYR A 472 -23.239 53.637 5.964 1.00 22.25 N

ANISOU 1236 N TYR A 472 3263 2445 2747 585 651 389 N

ATOM 1237 CA TYR A 472 -23.826 52.304 5.730 1.00 16.24 C

ANISOU 1237 CA TYR A 472 2498 1709 1962 580 614 386 C

ATOM 1238 CB TYR A 472 -24.020 51.572 7.071 1.00 18.23 C

ANISOU 1238 CB TYR A 472 2769 1948 2208 553 597 364 C

ATOM 1239 CG TYR A 472 -24.668 50.201 6.960 1.00 20.77 C

ANISOU 1239 CG TYR A 472 3088 2293 2509 543 555 363 C

ATOM 1240 CDl TYR A 472 -23.913 49.063 6.719 1.00 20.80 C

ANISOU 1240 CDl TYR A 472 3103 2304 2498 534 514 341 C

ATOM 1241 CE1 TYR A 472 -24.513 47.807 6.616 1.00 11.80 C

ANISOU 1241 CE1 TYR A 472 1963 1181 1339 524 471 340 C

ATOM 1242 CD2 TYR A 472 -26.043 50.054 7.101 1.00 23.11 C

ANISOU 1242 CD2 TYR A 472 3372 2605 2802 543 556 385 C

ATOM 1243 CE2 TYR A 472 -26.641 48.819 6.992 1.00 21.91 C

ANISOU 1243 CE2 TYR A 472 3218 2472 2634 531 514 388 C

ATOM 1244 CZ TYR A 472 -25.866 47.699 6.760 1.00 15.14 C ANISOU 1244 CZ TYR A 472 2374 1618 1761 521 470 364 C

ATOM 1245 OH TYR A 472 -26.483 46.474 6.655 1.00 21.29 O ANISOU 1245 OH TYR A 472 3153 2412 2523 508 424 367 O

ATOM 1246 C TYR A 472 -25.132 52.318 4.927 1.00 17.72 C

ANISOU 1246 C TYR A 472 2665 1924 2145 596 616 418 C

ATOM 1247 0 TYR A 472 -25.266 51.598 3.941 1.00 16.10 O

ANISOU 1247 O TYR A 472 2452 1743 1922 604 589 424 O

ATOM 1248 N ASP A 473 -26.076 53.160 5.348 1.00 14.14 N

ANISOU 1248 N ASP A 473 2203 1464 1705 602 648 437 N

ATOM 1249 CA ASP A 473 -27.376 53.281 4.699 1.00 17.42 C

ANISOU 1249 CA ASP A 473 2596 1902 2121 617 653 471 C

ATOM 1250 CB ASP A 473 -28.249 54.314 5.439 1.00 26.12 C

ANISOU 1250 CB ASP A 473 3692 2990 3242 624 694 488 C

ATOM 1251 CG ASP A 473 -28.597 53.879 6.848 1.00 38.80 C

ANISOU 1251 CG ASP A 473 5312 4585 4844 605 693 472 C ATOM 1252 ODl ASP A 473 -28.668 52.653 7.100 1.00 28.87 O ANISOU 1252 ODl ASP A 473 4059 3340 3570 586 656 461 O ATOM 1253 OD2 ASP A 473 -28.807 54.766 7.701 1.00 54.21 O ANISOU 1253 OD2 ASP A 473 7272 6515 6809 611 729 471 O

ATOM 1254 C ASP A 473 -27.283 53.654 3.221 1.00 13.82 C

ANISOU 1254 C ASP A 473 2124 1464 1664 639 654 493 C

ATOM 1255 O ASP A 473 -27.975 53.075 2.388 1.00 20.79 O

ANISOU 1255 0 ASP A 473 2994 2371 2533 645 631 511 O

ATOM 1256 N GLU A 474 -26.439 54.633 2.900 1.00 18.82 N

ANISOU 1256 N GLU A 474 2758 2083 2310 650 680 493 N

ATOM 1257 CA GLU A 474 -26.228 55.033 1.511 1.00 17.77 C ANISOU 1257 CA GLU A 474 2611 1967 2175 670 684 514 C

ATOM 1258 CB GLU A 474 -25.413 56.323 1.439 1.00 20.02 C ANISOU 1258 CB GLU A 474 2894 2230 2480 679 718 519 C

ATOM 1259 CG GLU A 474 -25.383 56.959 0.053 1.00 33.55 C ANISOU 1259 CG GLU A 474 4591 3962 4196 701 729 549 C ATOM 1260 CD GLU A 474 -24.265 57.972 -0.113 1.00 51.56 C ANISOU 1260 CD GLU A 474 6872 6226 6494 705 753 551 C ATOM 1261 OEl GLU A 474 -23.104 57.629 0.195 1.00 45.08 O ANISOU 1261 OEl GLU A 474 6062 5396 5670 694 744 528 O ATOM 1262 OE2 GLU A 474 -24.542 59.107 -0.567 1.00 59.40 O ANISOU 1262 OE2 GLU A 474 7851 7213 7505 719 780 579 O

ATOM 1263 C GLU A 474 -25.493 53.927 0.760 1.00 10.12 C

ANISOU 1263 C GLU A 474 1649 1018 1179 670 647 499 C

ATOM 1264 O GLU A 474 -25.715 53.715 -0.428 1.00 18.47 O

ANISOU 1264 0 GLU A 474 2697 2099 2222 685 635 516 O

ATOM 1265 N ARG A 475 -24.594 53.235 1.455 1.00 19.20 N

ANISOU 1265 N ARG A 475 2817 2156 2323 653 629 466 N

ATOM 1266 CA ARG A 475 -23.888 52.103 0.848 1.00 16.31 C ANISOU 1266 CA ARG A 475 2460 1807 1931 655 594 448 C

ATOM 1267 CB ARG A 475 -22.904 51.479 1.838 1.00 9.70 C ANISOU 1267 CB ARG A 475 1641 951 1094 634 578 413 C

ATOM 1268 CG ARG A 475 -21.966 50.424 1.211 1.00 15.94 C

ANISOU 1268 CG ARG A 475 2440 1755 1861 641 546 393 C

ATOM 1269 CD ARG A 475 -21.245 49.616 2.294 1.00 23.16 C

ANISOU 1269 CD ARG A 475 3373 2652 2776 617 522 359 C

ATOM 1270 NE ARG A 475 -20.475 50.465 3.206 1.00 14.97 N

ANISOU 1270 NE ARG A 475 2338 1585 1764 604 549 351 N

ATOM 1271 CZ ARG A 475 -20.067 50.085 4.419 1.00 15.36 C

ANISOU 1271 CZ ARG A 475 2403 1611 1820 579 537 326 C

ATOM 1272 NHl ARG A 475 -20.358 48.874 4.892 1.00 14.49 N ANISOU 1272 NHl ARG A 475 2306 1504 1694 563 499 307 N

ATOM 1273 NH2 ARG A 475 -19.366 50.920 5.162 1.00 27.51 N ANISOU 1273 NH2 ARG A 475 3948 3123 3383 568 559 321 N

ATOM 1274 C ARG A 475 -24.919 51.058 0.438 1.00 19.77 C

ANISOU 1274 C ARG A 475 2897 2266 2347 654 556 455 C

ATOM 1275 O ARG A 475 -24.890 50.545 -0.684 1.00 12.01 O

ANISOU 1275 0 ARG A 475 1915 1305 1342 669 535 461 O

ATOM 1276 N MET A 476 -25.834 50.750 1.358 1.00 15.45 N

ANISOU 1276 N MET A 476 2352 1714 1806 636 548 456 N

ATOM 1277 CA MET A 476 -26.836 49.724 1.107 1.00 15.71 C

ANISOU 1277 CA MET A 476 2383 1764 1821 630 509 466 C

ATOM 1278 CB MET A 476 -27.664 49.420 2.351 1.00 20.05 C

ANISOU 1278 CB MET A 476 2933 2306 2381 607 504 466 C

ATOM 1279 CG MET A 476 -26.915 48.734 3.479 1.00 19.67 C

ANISOU 1279 CG MET A 476 2905 2241 2330 583 488 430 C

ATOM 1280 SD MET A 476 -26.116 47.177 3.001 1.00 18.57 S

ANISOU 1280 SD MET A 476 2786 2108 2160 577 429 401 S

ATOM 1281 CE MET A 476 -24.429 47.737 2.821 1.00 16.22 C

ANISOU 1281 CE MET A 476 2497 1797 1868 590 453 376 C

ATOM 1282 C MET A 476 -27.747 50.165 -0.035 1.00 20.24 C

ANISOU 1282 C MET A 476 2939 2359 2394 649 513 503 C

ATOM 1283 O MET A 476 -28.145 49.351 -0.866 1.00 20.44 O

ANISOU 1283 0 MET A 476 2967 2402 2397 653 475 511 O

ATOM 1284 N LYS A 477 -28.084 51.450 -0.078 1.00 9.40 N

ANISOU 1284 N LYS A 477 1549 981 1044 661 557 526 N

ATOM 1285 CA LYS A 477 -28.934 51.958 -1.171 1.00 18.20 C

ANISOU 1285 CA LYS A 477 2644 2112 2159 679 563 564 C

ATOM 1286 CB LYS A 477 -29.387 53.404 -0.912 1.00 19.03 C

ANISOU 1286 CB LYS A 477 2730 2205 2295 689 613 588 C

ATOM 1287 CG LYS A 477 -30.502 53.524 0.127 1.00 29.11 C

ANISOU 1287 CG LYS A 477 3996 3476 3590 679 625 601 C

ATOM 1288 CD LYS A 477 -30.998 54.966 0.279 1.00 33.84 C

ANISOU 1288 CD LYS A 477 4577 4062 4217 695 674 625 C

ATOM 1289 CE LYS A 477 -32.282 55.003 1.096 1.00 50.38 C

ANISOU 1289 CE LYS A 477 6658 6159 6326 691 685 645 C

ATOM 1290 NZ LYS A 477 -32.763 56.388 1.371 1.00 58.54 N ANISOU 1290 NZ LYS A 477 7678 7178 7388 710 735 665 N

ATOM 1291 C LYS A 477 -28.237 51.859 -2.531 1.00 15.48 C

ANISOU 1291 C LYS A 477 2305 1783 1793 698 552 565 C

ATOM 1292 O LYS A 477 -28.847 51.476 -3.534 1.00 18.91 O

ANISOU 1292 0 LYS A 477 2737 2238 2211 707 526 585 O

ATOM 1293 N LYS A 478 -26.959 52.215 -2.565 1.00 16.23 N

ANISOU 1293 N LYS A 478 2409 1870 1889 704 571 545 N

ATOM 1294 CA LYS A 478 -26.186 52.112 -3.804 1.00 20.12 C

ANISOU 1294 CA LYS A 478 2906 2380 2359 725 564 546 C

ATOM 1295 CB LYS A 478 -24.815 52.784 -3.682 1.00 19.17 C

ANISOU 1295 CB LYS A 478 2787 2248 2250 730 595 532 C

ATOM 1296 CG LYS A 478 -24.070 52.808 -5.012 1.00 26.39 C

ANISOU 1296 CG LYS A 478 3701 3184 3141 754 597 540 C

ATOM 1297 CD LYS A 478 -22.820 53.648 -4.951 1.00 36.99 C

ANISOU 1297 CD LYS A 478 5037 4518 4501 760 631 538 C

ATOM 1298 CE LYS A 478 -22.236 53.836 -6.341 1.00 46.43 C

ANISOU 1298 CE LYS A 478 6227 5739 5674 786 639 555 C

ATOM 1299 NZ LYS A 478 -21.053 54.746 -6.337 1.00 40.38 N

ANISOU 1299 NZ LYS A 478 5448 4966 4928 790 673 561 N

ATOM 1300 C LYS A 478 -26.044 50.666 -4.289 1.00 15.23 C

ANISOU 1300 C LYS A 478 2308 1776 1704 725 514 526 C

ATOM 1301 O LYS A 478 -26.118 50.412 -5.490 1.00 15.85 O

ANISOU 1301 O LYS A 478 2391 1874 1757 744 498 538 O

ATOM 1302 N LEU A 479 -25.865 49.721 -3.364 1.00 17.82 N

ANISOU 1302 N LEU A 479 2650 2093 2028 706 487 497 N

ATOM 1303 CA LEU A 479 -25.756 48.310 -3.732 1.00 19.16 C

ANISOU 1303 CA LEU A 479 2843 2273 2166 705 435 477 C

ATOM 1304 CB LEU A 479 -25.529 47.435 -2.497 1.00 21.93 C

ANISOU 1304 CB LEU A 479 3206 2606 2520 680 411 447 C

ATOM 1305 CG LEU A 479 -24.150 47.404 -1.830 1.00 25.85 C

ANISOU 1305 CG LEU A 479 3711 3087 3022 675 424 414 C

ATOM 1306 CDl LEU A 479 -24.181 46.510 -0.561 1.00 20.53 C ANISOU 1306 CDl LEU A 479 3051 2397 2353 646 395 388 C

ATOM 1307 CD2 LEU A 479 -23.102 46.921 -2.807 1.00 17.27 C ANISOU 1307 CD2 LEU A 479 2638 2013 1909 700 412 398 C

ATOM 1308 C LEU A 479 -27.017 47.835 -4.440 1.00 22.94 C

ANISOU 1308 C LEU A 479 3321 2766 2629 706 400 502 C

ATOM 1309 O LEU A 479 -26.965 47.128 -5.455 1.00 10.69 O

ANISOU 1309 O LEU A 479 1787 1229 1046 721 366 500 O

ATOM 1310 N VAL A 480 -28.151 48.210 -3.867 1.00 20.12 N

ANISOU 1310 N VAL A 480 2945 2405 2294 691 408 527 N

ATOM 1311 CA VAL A 480 -29.452 47.868 -4.411 1.00 23.35 C ANISOU 1311 CA VAL A 480 3348 2827 2698 688 376 558 C

ATOM 1312 CB VAL A 480 -30.587 48.354 -3.469 1.00 21.06 C ANISOU 1312 CB VAL A 480 3032 2531 2440 670 394 584 C

ATOM 1313 CGI VAL A 480 -31.955 48.116 -4.102 1.00 31.04 C ANISOU 1313 CGI VAL A 480 4282 3809 3702 667 364 624 C ATOM 1314 CG2 VAL A 480 -30.486 47.645 -2.112 1.00 14.87 C ANISOU 1314 CG2 VAL A 480 2255 1732 1661 644 381 559 C ATOM 1315 C VAL A 480 -29.626 48.483 -5.795 1.00 17.51 C ANISOU 1315 C VAL A 480 2603 2104 1948 713 386 585 C ATOM 1316 O VAL A 480 -30.126 47.837 -6.714 1.00 21.22 O ANISOU 1316 0 VAL A 480 3084 2587 2393 719 344 597 O ATOM 1317 N SER A 481 -29.207 49.736 -5.935 1.00 18.88 N ANISOU 1317 N SER A 481 2759 2274 2138 727 438 595 N ATOM 1318 C SER A 481 -28.471 49.823 -8.271 1.00 19.39 C ANISOU 1318 C SER A 481 2843 2369 2156 770 430 606 C ATOM 1319 0 SER A 481 -28.890 49.690 -9.431 1.00 15.96 O ANISOU 1319 0 SER A 481 2415 1951 1697 784 409 626 O ATOM 1320 CA ASER A 481 -29.347 50.448 -7.195 0.50 16.81 C ANISOU 1320 CA ASER A 481 2490 2028 1870 750 452 624 C ATOM 1321 CB ASER A 481 -28.998 51.924 -7.024 0.50 16.41 C ANISOU 1321 CB ASER A 481 2417 1968 1848 759 511 638 C ATOM 1322 OG ASER A 481 -29.171 52.616 -8.247 0.50 21.61 O ANISOU 1322 OG ASER A 481 3067 2642 2500 779 523 668 O ATOM 1323 CA BSER A 481 -29.343 50.451 -7.195 0.50 16.78 C ANISOU 1323 CA BSER A 481 2486 2023 1865 750 452 624 C ATOM 1324 CB BSER A 481 -28.990 51.926 -7.014 0.50 16.38 C ANISOU 1324 CB BSER A 481 2414 1965 1845 759 511 637 C ATOM 1325 OG BSER A 481 -29.943 52.570 -6.189 0.50 24.19 O ANISOU 1325 OG BSER A 481 3381 2942 2869 747 532 658 O ATOM 1326 N ILE A 482 -27.263 49.430 -7.882 1.00 18.87 N ANISOU 1326 N ILE A 482 2792 2298 2081 772 434 570 N ATOM 1327 CA ILE A 482 -26.345 48.770 -8.793 1.00 20.31 C ANISOU 1327 CA ILE A 482 2998 2493 2224 794 416 550 C ATOM 1328 CB ILE A 482 -24.976 48.517 -8.115 1.00 25.38 C ANISOU 1328 CB ILE A 482 3648 3126 2868 794 430 513 C ATOM 1329 CG2 ILE A 482 -24.180 47.480 -8.895 1.00 24.88 C ANISOU 1329 CG2 ILE A 482 3615 3076 2762 817 400 487 C ATOM 1330 CGI ILE A 482 -24.208 49.835 -7.968 1.00 25.21 C ANISOU 1330 CGI ILE A 482 3603 3101 2874 800 488 524 C ATOM 1331 CD1 ILE A 482 -23.083 49.804 -6.938 1.00 22.30 C ANISOU 1331 CD 1 ILE A 482 3235 2714 2523 789 504 494 C ATOM 1332 C ILE A 482 -26.922 47.441 -9.311 1.00 24.89 C ANISOU 1332 C ILE A 482 3607 3081 2769 794 352 542 C ATOM 1333 0 ILE A 482 -26.890 47.167 -10.510 1.00 24.94 O ANISOU 1333 0 ILE A 482 3632 3104 2741 817 334 548 O ATOM 1334 N VAL A 483 -27.441 46.618 -8.404 1.00 24.07 N ANISOU 1334 N VAL A 483 3509 2964 2673 768 318 529 N ATOM 1335 CA VAL A 483 -28.080 45.352 -8.786 1.00 31.48 C ANISOU 1335 CA VAL A 483 4474 3904 3582 763 251 525 C ATOM 1336 CB VAL A 483 -28.466 44.513 -7.538 1.00 26.23 C ANISOU 1336 CB VAL A 483 3811 3223 2933 730 219 510 C ATOM 1337 CGI VAL A 483 -29.405 43.347 -7.915 1.00 10.67 C

ANISOU 1337 CGI VAL A 483 1861 1252 940 718 147 518 C ATOM 1338 CG2 VAL A 483 -27.218 44.012 -6.835 1.00 20.61 C ANISOU 1338 CG2 VAL A 483 3114 2500 2218 730 223 466 C

ATOM 1339 C VAL A 483 -29.317 45.569 -9.679 1.00 24.79 C

ANISOU 1339 C VAL A 483 3621 3068 2730 765 231 566 C

ATOM 1340 O VAL A 483 -29.517 44.872 -10.675 1.00 23.10 O

ANISOU 1340 O VAL A 483 3435 2862 2480 777 187 567 O

ATOM 1341 N ALA A 484 -30.149 46.539 -9.322 1.00 18.38 N

ANISOU 1341 N ALA A 484 2774 2255 1953 753 262 601 N ATOM 1342 CA ALA A 484 -31.313 46.859 -10.150 1.00 24.98 C

ANISOU 1342 CA ALA A 484 3600 3102 2791 754 247 645 C

ATOM 1343 CB ALA A 484 -32.081 48.023 -9.552 1.00 21.72 C

ANISOU 1343 CB ALA A 484 3144 2684 2422 744 291 679 C

ATOM 1344 C ALA A 484 -30.924 47.164 -11.602 1.00 33.40 C

ANISOU 1344 C ALA A 484 4683 4185 3825 785 250 653 C

ATOM 1345 0 ALA A 484 -31.568 46.681 -12.538 1.00 22.40 O

ANISOU 1345 O ALA A 484 3307 2799 2405 789 206 670 O

ATOM 1346 N ASP A 485 -29.873 47.969 -11.770 1.00 26.74 N

ANISOU 1346 N ASP A 485 3833 3346 2982 805 302 642 N

ATOM 1347 CA ASP A 485 -29.378 48.389 -13.083 1.00 28.43 C

ANISOU 1347 CA ASP A 485 4058 3578 3167 835 316 652 C

ATOM 1348 CB ASP A 485 -28.342 49.506 -12.924 1.00 28.40 C

ANISOU 1348 CB ASP A 485 4033 3576 3181 848 381 649 C

ATOM 1349 CG ASP A 485 -27.826 50.015 -14.250 1.00 44.17 C

ANISOU 1349 CG ASP A 485 6037 5594 5150 879 400 664 C ATOM 1350 ODl ASP A 485 -28.660 50.419 -15.085 1.00 56.12 O ANISOU 1350 ODl ASP A 485 7546 7117 6659 883 392 699 O ATOM 1351 OD2 ASP A 485 -26.591 50.022 -14.455 1.00 39.36 O ANISOU 1351 OD2 ASP A 485 5436 4994 4524 898 424 643 O

ATOM 1352 C ASP A 485 -28.758 47.230 -13.850 1.00 26.19 C

ANISOU 1352 C ASP A 485 3819 3303 2830 855 274 622 C

ATOM 1353 0 ASP A 485 -28.938 47.101 -15.062 1.00 36.40 O

ANISOU 1353 0 ASP A 485 5133 4610 4088 875 254 635 O

ATOM 1354 N GLN A 486 -28.030 46.377 -13.147 1.00 19.16 N

ANISOU 1354 N GLN A 486 2946 2403 1933 851 260 581 N ATOM 1355 CA GLN A 486 -27.402 45.239 -13.813 1.00 21.18 C

ANISOU 1355 CA GLN A 486 3245 2664 2138 873 220 550 C ATOM 1356 CB GLN A 486 -26.325 44.624 -12.924 1.00 19.54 C

ANISOU 1356 CB GLN A 486 3046 2446 1934 871 224 506 C ATOM 1357 CG GLN A 486 -25.043 45.447 -12.880 1.00 29.99 C

ANISOU 1357 CG GLN A 486 4351 3778 3266 890 287 498 C ATOM 1358 CD GLN A 486 -24.048 44.906 -11.884 1.00 31.55 C

ANISOU 1358 CD GLN A 486 4552 3962 3474 884 290 459 C ATOM 1359 OE1 GLN A 486 -24.430 44.337 -10.857 1.00 23.83 O ANISOU 1359 OEl GLN A 486 3574 2964 2514 855 263 445 O

ATOM 1360 NE2 GLN A 486 -22.765 45.077 -12.177 1.00 24.95 N

ANISOU 1360 NE2 GLN A 486 3717 3138 2627 910 323 444 N

ATOM 1361 C GLN A 486 -28.425 44.190 -14.267 1.00 20.48 C

ANISOU 1361 C GLN A 486 3188 2571 2024 864 146 555 C

ATOM 1362 0 GLN A 486 -28.330 43.653 -15.373 1.00 30.22 O

ANISOU 1362 0 GLN A 486 4458 3814 3210 888 115 550 O

ATOM 1363 N LEU A 487 -29.405 43.901 -13.422 1.00 24.53 N

ANISOU 1363 N LEU A 487 3686 3069 2566 829 118 567 N

ATOM 1364 CA LEU A 487 -30.462 42.971 -13.805 1.00 28.78 C

ANISOU 1364 CA LEU A 487 4248 3601 3086 815 45 580 C

ATOM 1365 CB LEU A 487 -31.410 42.715 -12.631 1.00 27.08 C

ANISOU 1365 CB LEU A 487 4008 3371 2911 774 24 595 C

ATOM 1366 CG LEU A 487 -30.874 41.857 -11.477 1.00 27.92 C

ANISOU 1366 CG LEU A 487 4122 3461 3024 756 8 557 C

ATOM 1367 CD 1 LEU A 487 -31.868 41.832 -10.328 1.00 14.50 C

ANISOU 1367 CD 1 LEU A 487 2391 1751 1366 717 -0 579 C

ATOM 1368 CD2 LEU A 487 -30.544 40.435 -11.938 1.00 24.69 C

ANISOU 1368 CD2 LEU A 487 3766 3044 2570 765 -60 524 C

ATOM 1369 C LEU A 487 -31.240 43.499 -15.009 1.00 36.38 C

ANISOU 1369 C LEU A 487 5212 4577 4035 826 37 621 C

ATOM 1370 O LEU A 487 -31.569 42.751 -15.930 1.00 33.76 O

ANISOU 1370 O LEU A 487 4919 4245 3663 835 -19 621 O

ATOM 1371 N GLU A 488 -31.531 44.794 -14.987 1.00 33.58 N

ANISOU 1371 N GLU A 488 4816 4230 3714 824 91 654 N

ATOM 1372 CA GLU A 488 -32.246 45.446 -16.074 1.00 39.85 C

ANISOU 1372 CA GLU A 488 5606 5037 4501 834 90 696 C

ATOM 1373 CB GLU A 488 -32.589 46.880 -15.676 1.00 29.45 C

ANISOU 1373 CB GLU A 488 4236 3722 3232 827 153 730 C

ATOM 1374 CG GLU A 488 -32.972 47.783 -16.838 1.00 53.76 C

ANISOU 1374 CG GLU A 488 7307 6816 6304 843 168 769 C

ATOM 1375 CD GLU A 488 -33.155 49.228 -16.407 1.00 56.15 C

ANISOU 1375 CD GLU A 488 7560 7119 6656 839 232 798 C

ATOM 1376 OEl GLU A 488 -33.524 49.455 -15.235 1.00 64.83 O

ANISOU 1376 OEl GLU A 488 8629 8205 7798 818 250 801 O

ATOM 1377 OE2 GLU A 488 -32.930 50.135 -17.235 1.00 52.09 O

ANISOU 1377 OE2 GLU A 488 7039 6617 6137 858 264 819 O

ATOM 1378 C GLU A 488 -31.450 45.430 -17.381 1.00 47.14 C

ANISOU 1378 C GLU A 488 6565 5976 5371 872 94 683 C

ATOM 1379 0 GLU A 488 -32.014 45.226 -18.455 1.00 51.38 O

ANISOU 1379 0 GLU A 488 7125 6518 5876 880 56 703 O

ATOM 1380 N LYS A 489 -30.141 45.638 -17.287 1.00 39.90 N

ANISOU 1380 N LYS A 489 5650 5066 4443 895 139 652 N

ATOM 1381 CA LYS A 489 -29.298 45.678 -18.477 1.00 32.64 C

ANISOU 1381 CA LYS A 489 4761 4167 3475 934 151 642 C

ATOM 1382 CB LYS A 489 -28.202 46.733 -18.322 1.00 32.09 C ANISOU 1382 CB LYS A 489 4661 4109 3422 951 228 640 C

ATOM 1383 CG LYS A 489 -28.736 48.145 -18.204 1.00 39.48 C

ANISOU 1383 CG LYS A 489 5550 5048 4403 938 274 684 C

ATOM 1384 CD LYS A 489 -27.625 49.150 -17.981 1.00 48.98 C

ANISOU 1384 CD LYS A 489 6725 6259 5626 951 343 682 C

ATOM 1385 CE LYS A 489 -28.179 50.563 -17.929 1.00 58.53 C

ANISOU 1385 CE LYS A 489 7892 7468 6879 939 385 725 C

ATOM 1386 NZ LYS A 489 -27.141 51.547 -17.519 1.00 66.75 N

ANISOU 1386 NZ LYS A 489 8905 8512 7947 945 448 724 N

ATOM 1387 C LYS A 489 -28.699 44.311 -18.796 1.00 43.45 C

ANISOU 1387 C LYS A 489 6184 5533 4792 954 104 599 C

ATOM 1388 0 LYS A 489 -27.800 44.192 -19.630 1.00 50.79 O

ANISOU 1388 0 LYS A 489 7141 6479 5678 991 118 581 O

ATOM 1389 N ASN A 490 -29.202 43.283 -18.119 1.00 46.27 N

ANISOU 1389 N ASN A 490 6556 5869 5155 929 48 583 N

ATOM 1390 CA ASN A 490 -28.820 41.901 -18.398 1.00 46.78 C

ANISOU 1390 CA ASN A 490 6677 5926 5173 944 -9 543 C

ATOM 1391 CB ASN A 490 -29.341 41.474 -19.772 1.00 58.62 C

ANISOU 1391 CB ASN A 490 8223 7431 6619 964 -60 555 C

ATOM 1392 CG ASN A 490 -29.473 39.970 -19.903 1.00 68.44 C

ANISOU 1392 CG ASN A 490 9524 8656 7825 965 -141 524 C

ATOM 1393 ODl ASN A 490 -30.306 39.349 -19.241 1.00 73.34 O

ANISOU 1393 ODl ASN A 490 10143 9255 8468 929 -193 530 O

ATOM 1394 ND2 ASN A 490 -28.653 39.375 -20.762 1.00 68.23 N

ANISOU 1394 ND2 ASN A 490 9549 8636 7738 1008 -152 491 N

ATOM 1395 C ASN A 490 -27.321 41.625 -18.308 1.00 53.92 C

ANISOU 1395 C ASN A 490 7595 6838 6055 977 24 499 C

ATOM 1396 0 ASN A 490 -26.764 40.907 -19.141 1.00 61.84 O

ANISOU 1396 0 ASN A 490 8646 7846 7004 1012 0 473 O

ATOM 1397 N ARG A 491 -26.668 42.198 -17.302 1.00 40.92 N

ANISOU 1397 N ARG A 491 5909 5190 4451 966 77 491 N

ATOM 1398 CA ARG A 491 -25.265 41.899 -17.038 1.00 37.84 C

ANISOU 1398 CA ARG A 491 5525 4803 4048 991 106 452 C

ATOM 1399 CB ARG A 491 -24.429 43.180 -17.038 1.00 47.80 C

ANISOU 1399 CB ARG A 491 6746 6083 5332 1004 186 467 C

ATOM 1400 CG ARG A 491 -24.510 43.981 -18.337 1.00 55.35 C

ANISOU 1400 CG ARG A 491 7703 7065 6262 1031 213 498 C

ATOM 1401 CD ARG A 491 -23.234 44.774 -18.563 1.00 63.06 C

ANISOU 1401 CD ARG A 491 8657 8064 7239 1058 281 499 C

ATOM 1402 NE ARG A 491 -22.078 43.889 -18.692 1.00 71.74 N

ANISOU 1402 NE ARG A 491 9785 9169 8302 1091 278 458 N

ATOM 1403 CZ ARG A 491 -20.827 44.244 -18.422 1.00 80.65 C

ANISOU 1403 CZ ARG A 491 10892 10309 9442 1107 329 448 C

ATOM 1404 NHl ARG A 491 -20.560 45.474 -18.000 1.00 86.20 N ANISOU 1404 NHl ARG A 491 11546 11016 10191 1092 384 475 N

ATOM 1405 NH2 ARG A 491 -19.842 43.367 -18.568 1.00 80.70 N ANISOU 1405 NH2 ARG A 491 10925 10322 9417 1139 322 412 N

ATOM 1406 C ARG A 491 -25.153 41.180 -15.695 1.00 28.37 C

ANISOU 1406 C ARG A 491 4321 3580 2878 961 83 424 C

ATOM 1407 O ARG A 491 -25.953 41.419 -14.798 1.00 32.75 O

ANISOU 1407 O ARG A 491 4848 4121 3476 922 78 441 O

ATOM 1408 N LEU A 492 -24.171 40.297 -15.560 1.00 31.86 N

ANISOU 1408 N LEU A 492 4790 4018 3297 982 70 381 N ATOM 1409 CA LEU A 492 -24.027 39.520 -14.333 1.00 34.10 C

ANISOU 1409 CA LEU A 492 5074 4278 3605 954 43 353 C ATOM 1410 CB LEU A 492 -22.824 38.579 -14.427 1.00 34.40 C

ANISOU 1410 CB LEU A 492 5146 4315 3611 987 32 307 C ATOM 1411 CG LEU A 492 -22.676 37.591 -13.272 1.00 23.43 C

ANISOU 1411 CG LEU A 492 3764 2899 2239 961 -8 275 C ATOM 1412 CDl LEU A 492 -23.745 36.522 -13.367 1.00 24.62 C ANISOU 1412 CDl LEU A 492 3952 3030 2372 941 -91 274 C ATOM 1413 CD2 LEU A 492 -21.286 36.959 -13.271 1.00 39.03 C

ANISOU 1413 CD2 LEU A 492 5759 4875 4194 995 -0 234 C

ATOM 1414 C LEU A 492 -23.888 40.448 -13.126 1.00 31.02 C

ANISOU 1414 C LEU A 492 4631 3882 3273 924 95 365 C

ATOM 1415 O LEU A 492 -22.979 41.274 -13.074 1.00 28.60 O

ANISOU 1415 O LEU A 492 4299 3587 2980 938 156 366 O

ATOM 1416 N PRO A 493 -24.806 40.328 -12.155 1.00 28.25 N

ANISOU 1416 N PRO A 493 4264 3513 2956 881 72 376 N ATOM 1417 CD PRO A 493 -26.045 39.525 -12.174 1.00 19.33 C

ANISOU 1417 CD PRO A 493 3153 2371 1820 857 3 387 C ATOM 1418 CA PRO A 493 -24.741 41.239 -11.004 1.00 24.91 C ANISOU 1418 CA PRO A 493 3796 3084 2586 853 121 387 C ATOM 1419 CB PRO A 493 -25.893 40.761 -10.113 1.00 20.76 C

ANISOU 1419 CB PRO A 493 3264 2540 2084 811 79 398 C ATOM 1420 CG PRO A 493 -26.884 40.143 -11.089 1.00 21.07 C

ANISOU 1420 CG PRO A 493 3332 2583 2092 815 20 415 C

ATOM 1421 C PRO A 493 -23.408 41.148 -10.270 1.00 17.12 C

ANISOU 1421 C PRO A 493 2804 2091 1611 859 149 354 C

ATOM 1422 0 PRO A 493 -22.830 40.071 -10.177 1.00 21.53 O

ANISOU 1422 0 PRO A 493 3392 2641 2148 868 114 319 O

ATOM 1423 N SER A 494 -22.941 42.279 -9.743 1.00 25.40 N

ANISOU 1423 N SER A 494 3816 3141 2695 853 210 366 N

ATOM 1424 CA SER A 494 -21.663 42.337 -9.029 1.00 22.85 C ANISOU 1424 CA SER A 494 3484 2812 2388 855 240 340 C

ATOM 1425 CB SER A 494 -21.073 43.753 -9.108 1.00 23.87 C

ANISOU 1425 CB SER A 494 3578 2951 2542 863 308 362 C ATOM 1426 OG SER A 494 -20.807 44.108 -10.459 1.00 23.38 O ANISOU 1426 OG SER A 494 3520 2914 2448 900 327 377 O

ATOM 1427 C SER A 494 -21.764 41.882 -7.560 1.00 15.40 C

ANISOU 1427 C SER A 494 2535 1842 1475 816 221 322 C

ATOM 1428 O SER A 494 -20.756 41.749 -6.884 1.00 18.65 O ANISOU 1428 0 SER A 494 2944 2245 1899 814 234 298 O

ATOM 1429 N VAL A 495 -22.984 41.682 -7.067 1.00 17.63 N

ANISOU 1429 N VAL A 495 2815 2115 1769 786 192 336 N

ATOM 1430 CA VAL A 495 -23.193 41.123 -5.723 1.00 13.78 C

ANISOU 1430 CA VAL A 495 2325 1605 1304 749 168 321 C

ATOM 1431 CB VAL A 495 -24.462 41.675 -5.059 1.00 21.79 C

ANISOU 1431 CB VAL A 495 3316 2615 2349 717 175 352 C

ATOM 1432 CGI VAL A 495 -24.812 40.887 -3.784 1.00 9.82 C

ANISOU 1432 CGI VAL A 495 1805 1080 848 680 140 338 C

ATOM 1433 CG2 VAL A 495 -24.283 43.152 -4.741 1.00 17.81 C ANISOU 1433 CG2 VAL A 495 2779 2112 1877 717 243 372 C

ATOM 1434 C VAL A 495 -23.308 39.620 -5.873 1.00 9.55 C

ANISOU 1434 C VAL A 495 1828 1063 739 749 98 296 C

ATOM 1435 O VAL A 495 -24.127 39.129 -6.644 1.00 18.19 O

ANISOU 1435 0 VAL A 495 2940 2162 1809 754 57 308 O

ATOM 1436 N HIS A 496 -22.455 38.887 -5.163 1.00 13.98 N

ANISOU 1436 N HIS A 496 2401 1609 1301 743 82 262 N

ATOM 1437 CA HIS A 496 -22.441 37.443 -5.285 1.00 16.70 C

ANISOU 1437 CA HIS A 496 2783 1943 1618 744 14 235 C

ATOM 1438 CB HIS A 496 -21.132 36.902 -4.715 1.00 8.25 C

ANISOU 1438 CB HIS A 496 1722 861 551 750 14 196 C

ATOM 1439 CG HIS A 496 -20.919 35.442 -4.969 1.00 10.03 C

ANISOU 1439 CG HIS A 496 1989 1076 745 761 -52 165 C

ATOM 1440 CD2 HIS A 496 -20.039 34.795 -5.775 1.00 12.64 C

ANISOU 1440 CD2 HIS A 496 2349 1411 1042 802 -67 137 C

ATOM 1441 ND1 HIS A 496 -21.648 34.463 -4.331 1.00 12.93 N

ANISOU 1441 ND1 HIS A 496 2373 1425 1115 728 -114 160 N

ATOM 1442 CE1 HIS A 496 -21.237 33.274 -4.740 1.00 16.98 C

ANISOU 1442 CE1 HIS A 496 2925 1928 1597 747 -167 129 C

ATOM 1443 NE2 HIS A 496 -20.266 33.448 -5.623 1.00 16.98 N

ANISOU 1443 NE2 HIS A 496 2936 1943 1575 794 -139 114 N

ATOM 1444 C HIS A 496 -23.679 36.856 -4.587 1.00 17.20 C

ANISOU 1444 C HIS A 496 2848 1994 1694 703 -35 248 C

ATOM 1445 O HIS A 496 -24.078 37.331 -3.521 1.00 14.47 O

ANISOU 1445 0 HIS A 496 2475 1640 1381 670 -14 262 O

ATOM 1446 N PRO A 497 -24.308 35.834 -5.195 1.00 15.77 N

ANISOU 1446 N PRO A 497 2698 1810 1484 705 -101 247 N

ATOM 1447 CD PRO A 497 -23.952 35.169 -6.457 1.00 19.77 C

ANISOU 1447 CD PRO A 497 3245 2322 1946 744 -133 230 C

ATOM 1448 CA PRO A 497 -25.538 35.277 -4.609 1.00 13.11 C

ANISOU 1448 CA PRO A 497 2359 1462 1158 665 -150 267 C

ATOM 1449 CB PRO A 497 -25.859 34.076 -5.514 1.00 18.74 C

ANISOU 1449 CB PRO A 497 3118 2171 1833 677 -227 258 C

ATOM 1450 CG PRO A 497 -24.621 33.836 -6.327 1.00 20.18 C

ANISOU 1450 CG PRO A 497 3329 2356 1982 724 -218 222 C

ATOM 1451 C PRO A 497 -25.345 34.810 -3.174 1.00 15.12 C ANISOU 1451 C PRO A 497 2607 1700 1439 629 -162 251 C

ATOM 1452 O PRO A 497 -26.278 34.886 -2.381 1.00 17.42 O

ANISOU 1452 0 PRO A 497 2878 1988 1754 592 -169 276 O

ATOM 1453 N HIS A 498 -24.154 34.329 -2.839 1.00 14.81 N

ANISOU 1453 N HIS A 498 2584 1649 1395 639 -163 212 N

ATOM 1454 CA HIS A 498 -23.912 33.861 -1.479 1.00 10.29 C

ANISOU 1454 CA HIS A 498 2007 1058 845 604 -177 196 C

ATOM 1455 CB HIS A 498 -22.618 33.059 -1.420 1.00 12.54 C

ANISOU 1455 CB HIS A 498 2319 1330 1117 622 -196 152 C

ATOM 1456 CG HIS A 498 -22.392 32.363 -0.110 1.00 24.06 C

ANISOU 1456 CG HIS A 498 3780 2768 2595 585 -224 134 C

ATOM 1457 CD2 HIS A 498 -21.307 32.311 0.699 1.00 23.81 C

ANISOU 1457 CD2 HIS A 498 3745 2723 2578 581 -207 107 C

ATOM 1458 NDl HIS A 498 -23.351 31.570 0.487 1.00 24.88 N

ANISOU 1458 NDl HIS A 498 3890 2860 2703 547 -281 145 N

ATOM 1459 CE1 HIS A 498 -22.873 31.076 1.614 1.00 28.82 C

ANISOU 1459 CE1 HIS A 498 4390 3341 3217 520 -295 126 C

ATOM 1460 NE2 HIS A 498 -21.634 31.510 1.767 1.00 24.12 N

ANISOU 1460 NE2 HIS A 498 3791 2744 2630 540 -252 101 N

ATOM 1461 C HIS A 498 -23.874 35.019 -0.480 1.00 16.77 C

ANISOU 1461 C HIS A 498 2789 1880 1703 584 -111 211 C

ATOM 1462 0 HIS A 498 -23.966 34.804 0.730 1.00 19.04 O

ANISOU 1462 0 HIS A 498 3069 2155 2011 549 -118 207 O

ATOM 1463 N HIS A 499 -23.733 36.242 -0.987 1.00 12.93 N

ANISOU 1463 N HIS A 499 2281 1410 1224 606 -50 227 N

ATOM 1464 CA HIS A 499 -23.668 37.415 -0.124 1.00 10.75 C

ANISOU 1464 CA HIS A 499 1972 1131 980 591 12 240 C

ATOM 1465 CB HIS A 499 -22.546 38.373 -0.572 1.00 11.67 C

ANISOU 1465 CB HIS A 499 2079 1254 1100 621 70 232 C

ATOM 1466 CG HIS A 499 -21.182 37.751 -0.590 1.00 16.22 C

ANISOU 1466 CG HIS A 499 2674 1823 1666 638 59 195 C

ATOM 1467 CD2 HIS A 499 -20.664 36.713 0.111 1.00 19.34 C

ANISOU 1467 CD2 HIS A 499 3088 2201 2061 623 19 165 C

ATOM 1468 NDl HIS A 499 -20.172 38.200 -1.416 1.00 15.04 N ANISOU 1468 NDl HIS A 499 2522 1685 1508 675 92 188 N

ATOM 1469 CE1 HIS A 499 -19.092 37.460 -1.227 1.00 15.28 C

ANISOU 1469 CE1 HIS A 499 2568 1706 1531 684 74 156 C

ATOM 1470 NE2 HIS A 499 -19.360 36.559 -0.298 1.00 18.23 N

ANISOU 1470 NE2 HIS A 499 2954 2060 1910 652 29 141 N

ATOM 1471 C HIS A 499 -24.988 38.194 -0.104 1.00 15.35 C

ANISOU 1471 C HIS A 499 2530 1725 1578 577 32 283 C

ATOM 1472 0 HIS A 499 -25.133 39.129 0.668 1.00 14.32 O

ANISOU 1472 O HIS A 499 2375 1593 1474 564 80 296 O

ATOM 1473 N SER A 500 -25.938 37.822 -0.960 1.00 14.26 N

ANISOU 1473 N SER A 500 2398 1598 1422 582 -3 305 N

ATOM 1474 CA SER A 500 -27.104 38.675 -1.205 1.00 9.69 C ANISOU 1474 CA SER A 500 1792 1032 857 579 21 348 C

ATOM 1475 CB SER A 500 -27.892 38.183 -2.420 1.00 18.37 C

ANISOU 1475 CB SER A 500 2905 2143 1931 591 -25 368 C

ATOM 1476 OG SER A 500 -28.536 36.955 -2.137 1.00 19.88 O

ANISOU 1476 OG SER A 500 3113 2325 2114 565 -95 369 O

ATOM 1477 C SER A 500 -28.020 38.803 0.023 1.00 13.37 C

ANISOU 1477 C SER A 500 2235 1494 1350 542 26 370 C

ATOM 1478 0 SER A 500 -28.776 39.777 0.163 1.00 11.96 O

ANISOU 1478 0 SER A 500 2027 1323 1192 539 67 402 O

ATOM 1479 N MET A 501 -27.927 37.842 0.932 1.00 15.79 N

ANISOU 1479 N MET A 501 2555 1788 1659 514 -13 352 N

ATOM 1480 CA MET A 501 -28.726 37.913 2.150 1.00 27.15 C

ANISOU 1480 CA MET A 501 3973 3224 3120 479 -6 372 C

ATOM 1481 CB MET A 501 -28.705 36.582 2.900 1.00 19.68 C

ANISOU 1481 CB MET A 501 3045 2264 2167 449 -67 355 C

ATOM 1482 CG MET A 501 -27.474 36.409 3.758 1.00 25.84 C

ANISOU 1482 CG MET A 501 3840 3027 2951 443 -56 314 C

ATOM 1483 SD MET A 501 -26.066 35.911 2.755 1.00 24.61 S

ANISOU 1483 SD MET A 501 3717 2864 2771 478 -75 271 S

ATOM 1484 CE MET A 501 -26.441 34.151 2.663 1.00 17.37 C ANISOU 1484 CE MET A 501 2831 1938 1833 458 -172 262 C

ATOM 1485 C MET A 501 -28.237 39.025 3.077 1.00 23.41 C

ANISOU 1485 C MET A 501 3481 2743 2669 478 63 365 C

ATOM 1486 0 MET A 501 -28.934 39.398 4.020 1.00 19.62 O

ANISOU 1486 0 MET A 501 2982 2263 2208 457 84 385 O

ATOM 1487 N LEU A 502 -27.040 39.553 2.823 1.00 13.26 N

ANISOU 1487 N LEU A 502 2204 1451 1383 501 96 339 N

ATOM 1488 CA LEU A 502 -26.469 40.555 3.719 1.00 9.00 C

ANISOU 1488 CA LEU A 502 1653 901 865 497 154 330 C

ATOM 1489 CB LEU A 502 -24.940 40.548 3.628 1.00 11.37 C

ANISOU 1489 CB LEU A 502 1970 1189 1162 511 163 293 C

ATOM 1490 CG LEU A 502 -24.247 39.209 3.942 1.00 17.71 C

ANISOU 1490 CG LEU A 502 2798 1979 1950 499 108 260 C

ATOM 1491 CDl LEU A 502 -22.756 39.311 3.693 1.00 16.16 C ANISOU 1491 CDl LEU A 502 2613 1776 1752 519 123 229 C

ATOM 1492 CD2 LEU A 502 -24.514 38.759 5.369 1.00 16.12 C

ANISOU 1492 CD2 LEU A 502 2600 1765 1761 460 93 254 C

ATOM 1493 C LEU A 502 -26.984 41.982 3.480 1.00 14.61 C

ANISOU 1493 C LEU A 502 2338 1620 1593 513 213 360 C

ATOM 1494 0 LEU A 502 -26.783 42.866 4.318 1.00 16.57 O

ANISOU 1494 0 LEU A 502 2577 1857 1861 507 259 358 O

ATOM 1495 N TYR A 503 -27.630 42.203 2.339 1.00 10.72 N

ANISOU 1495 N TYR A 503 1836 1145 1093 532 210 386 N

ATOM 1496 CA TYR A 503 -27.996 43.544 1.907 1.00 10.86 C ANISOU 1496 CA TYR A 503 1831 1170 1126 551 264 413 C

ATOM 1497 CB TYR A 503 -27.264 43.884 0.596 1.00 14.17 C ANISOU 1497 CB TYR A 503 2256 1598 1531 584 273 409 C

ATOM 1498 CG TYR A 503 -25.764 43.613 0.605 1.00 17.45 C ANISOU 1498 CG TYR A 503 2690 2002 1936 593 273 370 C ATOM 1499 CDl TYR A 503 -24.962 43.999 1.681 1.00 13.70 C ANISOU 1499 CDl TYR A 503 2216 1509 1480 580 301 349 C

ATOM 1500 CE1 TYR A 503 -23.585 43.753 1.677 1.00 14.99 C ANISOU 1500 CE1 TYR A 503 2393 1664 1639 587 300 318 C ATOM 1501 CD2 TYR A 503 -25.149 42.991 -0.472 1.00 17.63 C ANISOU 1501 CD2 TYR A 503 2732 2036 1933 615 246 356 C

ATOM 1502 CE2 TYR A 503 -23.781 42.755 -0.487 1.00 11.42 C ANISOU 1502 CE2 TYR A 503 1959 1242 1139 627 249 324 C

ATOM 1503 CZ TYR A 503 -23.008 43.137 0.581 1.00 17.79 C ANISOU 1503 CZ TYR A 503 2762 2031 1968 612 275 307 C

ATOM 1504 OH TYR A 503 -21.655 42.888 0.543 1.00 15.68 O ANISOU 1504 OH TYR A 503 2504 1757 1696 623 277 280 O

ATOM 1505 C TYR A 503 -29.506 43.568 1.667 1.00 17.30 C

ANISOU 1505 C TYR A 503 2626 2001 1947 546 253 455 C

ATOM 1506 O TYR A 503 -30.096 42.533 1.373 1.00 18.35 O

ANISOU 1506 O TYR A 503 2766 2141 2065 534 198 464 O

ATOM 1507 N PRO A 504 -30.141 44.743 1.798 1.00 16.78 N

ANISOU 1507 N PRO A 504 2535 1939 1903 553 302 484 N

ATOM 1508 CD PRO A 504 -29.553 46.048 2.137 1.00 19.80 C ANISOU 1508 CD PRO A 504 2910 2309 2303 567 364 478 C

ATOM 1509 CA PRO A 504 -31.616 44.789 1.758 1.00 15.75 C ANISOU 1509 CA PRO A 504 2380 1822 1782 546 295 528 C

ATOM 1510 CB PRO A 504 -31.935 46.139 2.397 1.00 24.76 C ANISOU 1510 CB PRO A 504 3499 2958 2950 554 361 544 C

ATOM 1511 CG PRO A 504 -30.741 46.983 2.091 1.00 21.12 C ANISOU 1511 CG PRO A 504 3049 2485 2491 574 398 520 C

ATOM 1512 C PRO A 504 -32.177 44.724 0.341 1.00 20.44 C

ANISOU 1512 C PRO A 504 2968 2432 2364 563 271 555 C

ATOM 1513 O PRO A 504 -32.931 45.607 -0.079 1.00 16.24 O

ANISOU 1513 0 PRO A 504 2412 1910 1848 575 299 590 O

ATOM 1514 N LEU A 505 -31.778 43.693 -0.394 1.00 23.82 N

ANISOU 1514 N LEU A 505 3422 2862 2765 564 217 538 N

ATOM 1515 CA LEU A 505 -32.307 43.425 -1.724 1.00 18.44 C ANISOU 1515 CA LEU A 505 2744 2195 2067 577 182 560 C

ATOM 1516 CB LEU A 505 -31.352 42.504 -2.510 1.00 15.77 C ANISOU 1516 CB LEU A 505 2444 1855 1694 589 139 526 C

ATOM 1517 CG LEU A 505 -29.927 43.000 -2.757 1.00 16.64 C ANISOU 1517 CG LEU A 505 2567 1960 1795 614 177 491 C ATOM 1518 CDl LEU A 505 -28.951 41.829 -3.029 1.00 13.61 C ANISOU 1518 CDl LEU A 505 2220 1570 1381 619 132 451 C ATOM 1519 CD2 LEU A 505 -29.908 44.008 -3.892 1.00 19.92 C ANISOU 1519 CD2 LEU A 505 2973 2388 2208 643 211 512 C

ATOM 1520 C LEU A 505 -33.660 42.743 -1.566 1.00 19.78 C ANISOU 1520 C LEU A 505 2900 2372 2242 553 137 597 C

ATOM 1521 O LEU A 505 -33.903 42.059 -0.570 1.00 21.89 O

ANISOU 1521 O LEU A 505 3167 2634 2515 526 116 592 O

ATOM 1522 N SER A 506 -34.547 42.921 -2.539 1.00 26.80 N

ANISOU 1522 N SER A 506 3778 3275 3131 561 121 635 N

ATOM 1523 CA SER A 506 -35.814 42.200 -2.515 1.00 27.50 C

ANISOU 1523 CA SER A 506 3853 3370 3225 537 70 673 C

ATOM 1524 CB SER A 506 -36.749 42.719 -3.610 1.00 19.53 C

ANISOU 1524 CB SER A 506 2825 2374 2220 549 65 719 C

ATOM 1525 OG SER A 506 -36.148 42.577 -4.882 1.00 21.06 O

ANISOU 1525 OG SER A 506 3049 2569 2383 571 44 701 O

ATOM 1526 C SER A 506 -35.546 40.701 -2.693 1.00 26.54 C

ANISOU 1526 C SER A 506 3768 3242 3076 520 -7 648 C

ATOM 1527 O SER A 506 -34.490 40.304 -3.176 1.00 19.15 O

ANISOU 1527 0 SER A 506 2867 2298 2112 536 -22 608 O

ATOM 1528 N HIS A 507 -36.489 39.864 -2.281 1.00 23.54 N

ANISOU 1528 N HIS A 507 3375 2864 2703 488 -56 671 N

ATOM 1529 CA HIS A 507 -36.365 38.429 -2.521 1.00 22.71 C

ANISOU 1529 CA HIS A 507 3303 2750 2574 469 -135 648 C

ATOM 1530 CB HIS A 507 -37.524 37.673 -1.866 1.00 23.52 C

ANISOU 1530 CB HIS A 507 3383 2857 2695 428 -181 683 C

ATOM 1531 CG HIS A 507 -37.624 37.899 -0.389 1.00 27.84 C

ANISOU 1531 CG HIS A 507 3907 3406 3267 410 -143 690 C

ATOM 1532 CD2 HIS A 507 -38.627 38.396 0.372 1.00 28.53 C

ANISOU 1532 CD2 HIS A 507 3951 3506 3384 397 -113 737 C

ATOM 1533 NDl HIS A 507 -36.587 37.620 0.476 1.00 30.18 N ANISOU 1533 NDl HIS A 507 4224 3687 3555 407 -131 647 N

ATOM 1534 CE1 HIS A 507 -36.952 37.925 1.710 1.00 37.96 C

ANISOU 1534 CE1 HIS A 507 5184 4676 4562 391 -97 665 C

ATOM 1535 NE2 HIS A 507 -38.188 38.389 1.676 1.00 28.31 N

ANISOU 1535 NE2 HIS A 507 3924 3472 3362 386 -84 720 N

ATOM 1536 C HIS A 507 -36.319 38.150 -4.018 1.00 24.59 C

ANISOU 1536 C HIS A 507 3568 2990 2785 487 -175 644 C

ATOM 1537 O HIS A 507 -35.650 37.211 -4.466 1.00 20.07 O

ANISOU 1537 0 HIS A 507 3038 2405 2181 492 -223 607 O

ATOM 1538 N GLY A 508 -37.035 38.974 -4.785 1.00 21.17 N

ANISOU 1538 N GLY A 508 3113 2570 2361 500 -154 682 N

ATOM 1539 CA GLY A 508 -37.032 38.873 -6.233 1.00 23.00 C ANISOU 1539 CA GLY A 508 3369 2803 2565 520 -185 682 C

ATOM 1540 C GLY A 508 -35.644 39.095 -6.802 1.00 23.99 C

ANISOU 1540 C GLY A 508 3531 2924 2659 558 -159 638 C

ATOM 1541 O GLY A 508 -35.185 38.339 -7.663 1.00 25.41 O

ANISOU 1541 O GLY A 508 3755 3099 2803 571 -206 612 O

ATOM 1542 N PHE A 509 -34.969 40.132 -6.316 1.00 16.41 N

ANISOU 1542 N PHE A 509 2554 1967 1713 576 -86 630 N

ATOM 1543 CA PHE A 509 -33.605 40.432 -6.759 1.00 14.68 C ANISOU 1543 CA PHE A 509 2363 1745 1470 610 -55 594 C

ATOM 1544 CB PHE A 509 -33.113 41.750 -6.167 1.00 14.59 C

ANISOU 1544 CB PHE A 509 2321 1736 1485 622 28 594 C

ATOM 1545 CG PHE A 509 -33.515 42.957 -6.953 1.00 24.33 C

ANISOU 1545 CG PHE A 509 3532 2982 2729 642 70 628 C

ATOM 1546 CDl PHE A 509 -34.518 42.885 -7.897 1.00 24.49 C

ANISOU 1546 CDl PHE A 509 3551 3013 2743 642 36 666 C

ATOM 1547 CD2 PHE A 509 -32.876 44.169 -6.748 1.00 41.49 C

ANISOU 1547 CD2 PHE A 509 5687 5157 4920 659 142 622 C

ATOM 1548 CE1 PHE A 509 -34.889 44.009 -8.621 1.00 30.45 C

ANISOU 1548 CE1 PHE A 509 4284 3778 3508 660 73 699 C

ATOM 1549 CE2 PHE A 509 -33.230 45.290 -7.472 1.00 33.82 C

ANISOU 1549 CE2 PHE A 509 4695 4196 3959 676 179 654 C

ATOM 1550 CZ PHE A 509 -34.241 45.211 -8.407 1.00 36.92 C

ANISOU 1550 CZ PHE A 509 5084 4598 4345 677 145 692 C

ATOM 1551 C PHE A 509 -32.640 39.324 -6.348 1.00 12.53 C

ANISOU 1551 C PHE A 509 2128 1459 1176 608 -90 545 C

ATOM 1552 O PHE A 509 -31.763 38.941 -7.115 1.00 19.16 O

ANISOU 1552 0 PHE A 509 3003 2296 1980 635 -104 516 O

ATOM 1553 N ARG A 510 -32.797 38.825 -5.126 1.00 16.14 N

ANISOU 1553 N ARG A 510 2575 1907 1653 577 -102 538 N

ATOM 1554 CA ARG A 510 -31.908 37.779 -4.626 1.00 20.99 C

ANISOU 1554 CA ARG A 510 3221 2504 2249 571 -136 494 C

ATOM 1555 CB ARG A 510 -32.168 37.491 -3.143 1.00 23.68 C

ANISOU 1555 CB ARG A 510 3542 2837 2617 535 -135 494 C

ATOM 1556 CG ARG A 510 -31.859 38.662 -2.209 1.00 23.55 C

ANISOU 1556 CG ARG A 510 3494 2822 2631 535 -56 496 C

ATOM 1557 CD ARG A 510 -31.637 38.174 -0.773 1.00 28.02 C

ANISOU 1557 CD ARG A 510 4058 3376 3212 505 -60 478 C

ATOM 1558 NE ARG A 510 -31.567 39.268 0.196 1.00 22.21 N

ANISOU 1558 NE ARG A 510 3293 2641 2505 501 10 483 N

ATOM 1559 CZ ARG A 510 -32.594 39.677 0.931 1.00 19.06 C

ANISOU 1559 CZ ARG A 510 2862 2248 2130 482 30 518 C

ATOM 1560 NHl ARG A 510 -33.771 39.091 0.801 1.00 18.35 N

ANISOU 1560 NHl ARG A 510 2762 2168 2044 462 -15 555 N

ATOM 1561 NH2 ARG A 510 -32.443 40.673 1.795 1.00 22.30 N

ANISOU 1561 NH2 ARG A 510 3254 2656 2563 482 94 518 N

ATOM 1562 C ARG A 510 -32.054 36.512 -5.462 1.00 11.69 C

ANISOU 1562 C ARG A 510 2083 1320 1038 571 -216 479 C

ATOM 1563 O ARG A 510 -31.068 35.880 -5.826 1.00 13.04 O

ANISOU 1563 0 ARG A 510 2292 1482 1179 592 -237 440 O

ATOM 1564 N LYS A 511 -33.289 36.149 -5.784 1.00 19.09 N

ANISOU 1564 N LYS A 511 3011 2261 1981 547 -261 511 N

ATOM 1565 CA LYS A 511 -33.514 34.988 -6.638 1.00 24.83 C

ANISOU 1565 CA LYS A 511 3779 2977 2677 545 -342 500 C

ATOM 1566 CB LYS A 511 -35.004 34.636 -6.709 1.00 19.85 C ANISOU 1566 CB LYS A 511 3129 2348 2065 508 -391 544 C

ATOM 1567 CG LYS A 511 -35.288 33.358 -7.513 1.00 21.94 C

ANISOU 1567 CG LYS A 511 3440 2595 2300 500 -484 533 C

ATOM 1568 CD LYS A 511 -36.707 32.829 -7.295 1.00 16.20 C

ANISOU 1568 CD LYS A 511 2691 1866 1599 453 -541 577 C

ATOM 1569 CE LYS A 511 -37.767 33.813 -7.765 1.00 25.50 C

ANISOU 1569 CE LYS A 511 3827 3063 2798 450 -514 633 C

ATOM 1570 NZ LYS A 511 -39.138 33.196 -7.768 1.00 29.39 N

ANISOU 1570 NZ LYS A 511 4302 3552 3312 407 -581 680 N

ATOM 1571 C LYS A 511 -32.944 35.225 -8.044 1.00 17.93 C

ANISOU 1571 C LYS A 511 2939 2109 1764 590 -338 487 C

ATOM 1572 O LYS A 511 -32.347 34.326 -8.644 1.00 17.11 O

ANISOU 1572 0 LYS A 511 2885 1994 1624 609 -384 453 O

ATOM 1573 N ALA A 512 -33.122 36.441 -8.560 1.00 16.49 N

ANISOU 1573 N ALA A 512 2732 1944 1590 610 -282 515 N

ATOM 1574 CA ALA A 512 -32.646 36.782 -9.902 1.00 16.12 C

ANISOU 1574 CA ALA A 512 2713 1906 1507 652 -273 510 C

ATOM 1575 CB ALA A 512 -33.179 38.158 -10.322 1.00 14.47 C

ANISOU 1575 CB ALA A 512 2465 1716 1317 661 -216 553 C

ATOM 1576 C ALA A 512 -31.126 36.748 -10.016 1.00 13.88 C

ANISOU 1576 C ALA A 512 2458 1622 1195 691 -244 467 C

ATOM 1577 0 ALA A 512 -30.582 36.334 -11.045 1.00 16.15 O

ANISOU 1577 0 ALA A 512 2788 1910 1438 725 -267 448 O

ATOM 1578 N ILE A 513 -30.436 37.223 -8.986 1.00 17.35 N

ANISOU 1578 N ILE A 513 2872 2060 1661 686 -191 453 N

ATOM 1579 CA ILE A 513 -28.974 37.095 -8.952 1.00 15.84 C

ANISOU 1579 CA ILE A 513 2699 1867 1452 714 -164 406 C

ATOM 1580 CB ILE A 513 -28.368 37.692 -7.669 1.00 16.14 C

ANISOU 1580 CB ILE A 513 2704 1901 1528 699 -106 394 C

ATOM 1581 CG2 ILE A 513 -26.860 37.330 -7.566 1.00 11.40 C

ANISOU 1581 CG2 ILE A 513 2124 1295 911 723 -92 346 C

ATOM 1582 CGI ILE A 513 -28.587 39.209 -7.641 1.00 19.82 C

ANISOU 1582 CGI ILE A 513 3126 2381 2023 702 -33 426 C

ATOM 1583 CD1 ILE A 513 -28.436 39.844 -6.260 1.00 16.83 C

ANISOU 1583 CD1 ILE A 513 2713 1994 1686 678 14 425 C

ATOM 1584 C ILE A 513 -28.576 35.621 -9.041 1.00 16.71 C

ANISOU 1584 C ILE A 513 2859 1960 1530 717 -234 369 C

ATOM 1585 O ILE A 513 -27.711 35.242 -9.832 1.00 14.81 O

ANISOU 1585 0 ILE A 513 2655 1722 1252 755 -241 338 O

ATOM 1586 N ALA A 514 -29.216 34.791 -8.223 1.00 14.54 N

ANISOU 1586 N ALA A 514 2585 1669 1270 680 -287 373 N

ATOM 1587 CA ALA A 514 -28.921 33.364 -8.229 1.00 14.64 C

ANISOU 1587 CA ALA A 514 2644 1662 1257 678 -360 339 C

ATOM 1588 CB ALA A 514 -29.762 32.632 -7.180 1.00 17.01 C

ANISOU 1588 CB ALA A 514 2930 1947 1587 624 -406 345 C

ATOM 1589 C ALA A 514 -29.144 32.772 -9.613 1.00 17.56 C ANISOU 1589 C ALA A 514 3060 2030 1580 704 -413 333 C

ATOM 1590 O ALA A 514 -28.314 32.004 -10.113 1.00 18.93 O

ANISOU 1590 O ALA A 514 3282 2195 1715 736 -442 297 O

ATOM 1591 N GLU A 515 -30.265 33.130 -10.235 1.00 16.16 N

ANISOU 1591 N GLU A 515 3031 1992 1117 616 -333 197 N

ATOM 1592 C GLU A 515 -29.543 32.989 -12.601 1.00 16.62 C

ANISOU 1592 C GLU A 515 3253 2019 1043 694 -329 198 C

ATOM 1593 0 GLU A 515 -29.270 32.218 -13.529 1.00 22.64 O

ANISOU 1593 0 GLU A 515 4089 2766 1748 722 -347 185 O

ATOM 1594 CA AGLU A 515 -30.601 32.619 -11.564 0.50 19.86 C

ANISOU 1594 CA AGLU A 515 3583 2441 1522 653 -387 187 C

ATOM 1595 CB AGLU A 515 -31.972 33.136 -12.005 0.50 23.71 C

ANISOU 1595 CB AGLU A 515 4074 2921 2013 663 -460 192 C

ATOM 1596 CG AGLU A 515 -32.492 32.524 -13.299 0.50 29.49 C

ANISOU 1596 CG AGLU A 515 4889 3632 2686 698 -533 178 C

ATOM 1597 CD AGLU A 515 -31.995 33.230 -14.549 0.50 38.12 C

ANISOU 1597 CD AGLU A 515 6073 4709 3702 748 -505 194 C

ATOM 1598 OEIAGLU A 515 -31.272 34.243 -14.434 0.50 36.66 O

ANISOU 1598 OEIAGLU A 515 5884 4529 3514 755 -427 217 O

ATOM 1599 OE2AGLU A 515 -32.342 32.770 -15.657 0.50 52.50 O

ANISOU 1599 OE2AGLU A 515 7972 6510 5466 780 -561 183 O

ATOM 1600 CA BGLU A 515 -30.592 32.607 -11.560 0.50 19.81 C

ANISOU 1600 CA BGLU A 515 3576 2434 1515 653 -387 186 C

ATOM 1601 CB BGLU A 515 -31.973 33.082 -12.012 0.50 23.55 C

ANISOU 1601 CB BGLU A 515 4055 2901 1993 663 -462 191 C

ATOM 1602 CG BGLU A 515 -32.349 32.621 -13.413 0.50 27.62 C

ANISOU 1602 CG BGLU A 515 4660 3393 2439 703 -524 180 C

ATOM 1603 CD BGLU A 515 -33.695 33.152 -13.862 0.50 34.62 C

ANISOU 1603 CD BGLU A 515 5549 4273 3331 715 -600 186 C

ATOM 1604 OEIBGLU A 515 -34.091 34.240 -13.393 0.50 40.01 O

ANISOU 1604 OEIBGLU A 515 6185 4965 4051 708 -583 207 O

ATOM 1605 OE2BGLU A 515 -34.355 32.486 -14.687 0.50 47.89 O

ANISOU 1605 OE2BGLU A 515 7280 5938 4980 733 -680 169 O

ATOM 1606 N ARG A 516 -28.960 34.178 -12.459 1.00 16.92 N

ANISOU 1606 N ARG A 516 3280 2063 1085 698 -259 223 N

ATOM 1607 CA ARG A 516 -27.927 34.611 -13.402 1.00 22.16 C

ANISOU 1607 CA ARG A 516 4016 2714 1689 736 -194 236 C

ATOM 1608 CB ARG A 516 -27.537 36.071 -13.177 1.00 24.14 C

ANISOU 1608 CB ARG A 516 4246 2970 1955 735 -125 265 C

ATOM 1609 CG ARG A 516 -28.631 37.067 -13.507 1.00 26.72 C

ANISOU 1609 CG ARG A 516 4581 3291 2279 749 -165 280 C

ATOM 1610 CD ARG A 516 -29.058 36.949 -14.962 1.00 41.09 C

ANISOU 1610 CD ARG A 516 6500 5087 4024 797 -211 279 C

ATOM 1611 NE ARG A 516 -30.086 37.925 -15.310 1.00 59.11 N

ANISOU 1611 NE ARG A 516 8791 7363 6303 814 -251 295 N

ATOM 1612 CZ ARG A 516 -29.832 39.133 -15.806 1.00 66.71 C ANISOU 1612 CZ ARG A 516 9791 8317 7239 840 -202 321 C ATOM 1613 NHl ARG A 516 -28.579 39.517 -16.013 1.00 72.94 N ANISOU 1613 NHl ARG A 516 10608 9102 8005 850 -110 334 N ATOM 1614 NH2 ARG A 516 -30.831 39.957 -16.094 1.00 52.25 N ANISOU 1614 NH2 ARG A 516 7966 6480 5407 856 -244 334 N

ATOM 1615 C ARG A 516 -26.707 33.709 -13.278 1.00 27.09 C

ANISOU 1615 C ARG A 516 4649 3340 2304 733 -144 225 C

ATOM 1616 0 ARG A 516 -26.037 33.411 -14.266 1.00 20.35 O

ANISOU 1616 0 ARG A 516 3872 2471 1390 769 -119 225 O

ATOM 1617 N HIS A 517 -26.419 33.267 -12.058 1.00 19.87 N

ANISOU 1617 N HIS A 517 3657 2445 1448 693 -130 216 N

ATOM 1618 CA HIS A 517 -25.299 32.358 -11.850 1.00 25.62 C

ANISOU 1618 CA HIS A 517 4386 3176 2172 690 -88 205 C

ATOM 1619 CB HIS A 517 -24.911 32.319 -10.375 1.00 23.68 C

ANISOU 1619 CB HIS A 517 4047 2953 1997 645 -58 202 C

ATOM 1620 CG HIS A 517 -24.086 33.490 -9.954 1.00 16.64 C

ANISOU 1620 CG HIS A 517 3123 2071 1130 637 21 225 C

ATOM 1621 CD2 HIS A 517 -24.403 34.797 -9.810 1.00 21.66 C

ANISOU 1621 CD2 HIS A 517 3740 2709 1783 632 40 246 C

ATOM 1622 ND1 HIS A 517 -22.739 33.388 -9.680 1.00 30.26 N

ANISOU 1622 ND1 HIS A 517 4833 3801 2862 634 93 229 N

ATOM 1623 CE1 HIS A 517 -22.268 34.579 -9.360 1.00 21.51 C

ANISOU 1623 CE1 HIS A 517 3696 2699 1778 625 151 249 C

ATOM 1624 NE2 HIS A 517 -23.257 35.452 -9.436 1.00 25.37 N

ANISOU 1624 NE2 HIS A 517 4185 3186 2271 623 122 260 N

ATOM 1625 C HIS A 517 -25.608 30.967 -12.379 1.00 29.68 C

ANISOU 1625 C HIS A 517 4948 3678 2653 702 -148 179 C

ATOM 1626 O HIS A 517 -24.743 30.306 -12.952 1.00 31.73 O

ANISOU 1626 0 HIS A 517 5258 3927 2872 726 -117 173 O

ATOM 1627 N GLY A 518 -26.849 30.529 -12.191 1.00 21.62 N

ANISOU 1627 N GLY A 518 3908 2655 1650 686 -232 164 N ATOM 1628 CA GLY A 518 -27.294 29.274 -12.760 1.00 23.67 C ANISOU 1628 CA GLY A 518 4217 2899 1877 697 -298 140 C

ATOM 1629 C GLY A 518 -27.096 29.297 -14.264 1.00 27.49 C

ANISOU 1629 C GLY A 518 4808 3359 2279 748 -301 142 C

ATOM 1630 O GLY A 518 -26.592 28.339 -14.846 1.00 26.91 O

ANISOU 1630 O GLY A 518 4794 3271 2161 768 -301 128 O

ATOM 1631 N ASN A 519 -27.485 30.405 -14.891 1.00 25.05 N

ANISOU 1631 N ASN A 519 4528 3043 1946 770 -302 161 N ATOM 1632 CA ASN A 519 -27.340 30.567 -16.343 1.00 20.32 C ANISOU 1632 CA ASN A 519 4038 2419 1264 822 -304 166 C ATOM 1633 CB ASN A 519 -27.967 31.888 -16.801 1.00 33.07 C ANISOU 1633 CB ASN A 519 5668 4030 2867 840 -313 189 C ATOM 1634 CG ASN A 519 -29.482 31.865 -16.755 1.00 57.38 C ANISOU 1634 CG ASN A 519 8726 7109 5969 828 -415 179 C ATOM 1635 OD1 ASN A 519 -30.097 30.813 -16.567 1.00 58.07 O ANISOU 1635 ODl ASN A 519 8799 7194 6071 811 -485 155 O ATOM 1636 ND2 ASN A 519 -30.095 33.031 -16.934 1.00 65.80 N ANISOU 1636 ND2 ASN A 519 9787 8176 7039 839 -425 199 N

ATOM 1637 C ASN A 519 -25.897 30.504 -16.836 1.00 21.03 C

ANISOU 1637 C ASN A 519 4179 2501 1312 850 -212 175 C

ATOM 1638 O ASN A 519 -25.637 30.059 -17.956 1.00 29.84 O

ANISOU 1638 0 ASN A 519 5390 3591 2355 891 -216 170 O

ATOM 1639 N LEU A 520 -24.965 30.976 -16.015 1.00 29.61 N

ANISOU 1639 N LEU A 520 5204 3606 2442 829 -131 189 N

ATOM 1640 CA LEU A 520 -23.545 30.854 -16.333 1.00 29.25 C

ANISOU 1640 CA LEU A 520 5190 3555 2370 851 -41 198 C

ATOM 1641 CB LEU A 520 -22.681 31.462 -15.227 1.00 29.66 C

ANISOU 1641 CB LEU A 520 5153 3630 2486 818 36 212 C

ATOM 1642 CG LEU A 520 -22.611 32.984 -15.115 1.00 39.54 C

ANISOU 1642 CG LEU A 520 6381 4886 3756 816 84 240 C ATOM 1643 CDl LEU A 520 -21.753 33.374 -13.921 1.00 34.90 C ANISOU 1643 CDl LEU A 520 5703 4322 3236 778 149 248 C ATOM 1644 CD2 LEU A 520 -22.056 33.586 -16.400 1.00 49.52 C ANISOU 1644 CD2 LEU A 520 7736 6126 4952 864 137 259 C

ATOM 1645 C LEU A 520 -23.164 29.391 -16.522 1.00 34.73 C

ANISOU 1645 C LEU A 520 5917 4238 3039 859 -57 174 C

ATOM 1646 0 LEU A 520 -22.426 29.046 -17.448 1.00 28.68 O

ANISOU 1646 0 LEU A 520 5230 3452 2215 898 -18 175 O

ATOM 1647 N CYS A 521 -23.662 28.534 -15.633 1.00 27.43 N

ANISOU 1647 N CYS A 521 4934 3328 2161 822 -110 152 N

ATOM 1648 C A CYS A 521 -23.374 27.105 -15.709 1.00 25.83 C

ANISOU 1648 CA CYS A 521 4759 3117 1941 826 -129 128 C

ATOM 1649 CB CYS A 521 -23.899 26.391 -14.463 1.00 29.53 C

ANISOU 1649 CB CYS A 521 5142 3604 2475 778 -176 110 C

ATOM 1650 SG CYS A 521 -23.152 26.988 -12.933 1.00 32.18 S

ANISOU 1650 SG CYS A 521 5362 3972 2894 736 -106 124 S

ATOM 1651 C CYS A 521 -23.979 26.482 -16.967 1.00 26.26 C

ANISOU 1651 C CYS A 521 4918 3141 1921 862 -193 114 C

ATOM 1652 0 CYS A 521 -23.347 25.663 -17.625 1.00 29.03 O

ANISOU 1652 0 CYS A 521 5337 3473 2222 891 -175 104 O

ATOM 1653 N LEU A 522 -25.211 26.865 -17.285 1.00 27.62 N

ANISOU 1653 N LEU A 522 5101 3307 2087 861 -270 111 N

ATOM 1654 CA LEU A 522 -25.878 26.364 -18.487 1.00 32.39 C

ANISOU 1654 CA LEU A 522 5804 3881 2620 894 -341 97 C

ATOM 1655 CB LEU A 522 -27.312 26.889 -18.569 1.00 31.88 C

ANISOU 1655 CB LEU A 522 5725 3817 2571 884 -430 95 C

ATOM 1656 CG LEU A 522 -28.349 26.136 -17.734 1.00 37.49 C

ANISOU 1656 CG LEU A 522 6366 4537 3341 839 -513 73 C ATOM 1657 CDl LEU A 522 -29.615 26.963 -17.555 1.00 48.14 C

ANISOU 1657 CDl LEU A 522 7671 5894 4725 824 -577 80 C ATOM 1658 CD2 LEU A 522 -28.660 24.787 -18.366 1.00 29.59 C ANISOU 1658 CD2 LEU A 522 5433 3511 2297 849 -581 43 C

ATOM 1659 C LEU A 522 -25.110 26.751 -19.743 1.00 34.67 C

ANISOU 1659 C LEU A 522 6198 4145 2828 950 -285 112 C

ATOM 1660 O LEU A 522 -24.917 25.932 -20.644 1.00 31.47 O

ANISOU 1660 O LEU A 522 5886 3714 2358 982 -300 98 O

ATOM 1661 N ASP A 523 -24.678 28.006 -19.799 1.00 32.60 N

ANISOU 1661 N ASP A 523 5926 3891 2570 960 -218 140 N

ATOM 1662 C A ASP A 523 -23.896 28.493 -20.926 1.00 39.65 C

ANISOU 1662 CA ASP A 523 6914 4760 3392 1012 -152 158 C

ATOM 1663 CB ASP A 523 -23.524 29.963 -20.731 1.00 39.60 C

ANISOU 1663 CB ASP A 523 6873 4766 3409 1011 -81 190 C

ATOM 1664 CG ASP A 523 -24.693 30.895 -20.965 1.00 42.97 C

ANISOU 1664 CG ASP A 523 7302 5191 3833 1013 -142 199 C

ATOM 1665 OD1 ASP A 523 -24.539 32.109 -20.709 1.00 43.88 O ANISOU 1665 OD1 ASP A 523 7383 5317 3974 1008 -93 224 O

ATOM 1666 OD2 ASP A 523 -25.762 30.417 -21.405 1.00 42.07 O ANISOU 1666 OD2 ASP A 523 7225 5065 3694 1020 -241 181 O

ATOM 1667 C ASP A 523 -22.638 27.660 -21.103 1.00 33.62 C

ANISOU 1667 C ASP A 523 6183 3986 2604 1029 -81 154 C

ATOM 1668 O ASP A 523 -22.301 27.261 -22.216 1.00 37.38 O

ANISOU 1668 O ASP A 523 6767 4433 3004 1075 -70 152 O

ATOM 1669 N LYS A 524 -21.948 27.401 -19.998 1.00 27.20 N

ANISOU 1669 N LYS A 524 5279 3199 1857 995 -34 154 N

ATOM 1670 CA LYS A 524 -20.717 26.619 -20.038 1.00 28.52 C

ANISOU 1670 CA LYS A 524 5463 3361 2013 1009 35 151 C

ATOM 1671 CB LYS A 524 -20.060 26.548 -18.656 1.00 37.64 C

ANISOU 1671 CB LYS A 524 6501 4548 3252 966 80 153 C

ATOM 1672 CG LYS A 524 -19.403 27.844 -18.193 1.00 50.61 C

ANISOU 1672 CG LYS A 524 8083 6208 4937 954 161 182 C

ATOM 1673 CD LYS A 524 -18.512 27.592 -16.981 1.00 59.12 C

ANISOU 1673 CD LYS A 524 9063 7313 6086 920 212 182 C

ATOM 1674 CE LYS A 524 -17.866 28.875 -16.462 1.00 62.73 C

ANISOU 1674 CE LYS A 524 9456 7787 6591 903 287 208 C

ATOM 1675 NZ LYS A 524 -18.787 29.694 -15.621 1.00 50.59 N

ANISOU 1675 NZ LYS A 524 7848 6270 5105 863 243 211 N

ATOM 1676 C LYS A 524 -20.932 25.211 -20.589 1.00 37.40 C

ANISOU 1676 C LYS A 524 6660 4462 3088 1027 -19 123 C

ATOM 1677 0 LYS A 524 -20.110 24.720 -21.362 1.00 46.60 O

ANISOU 1677 O LYS A 524 7903 5605 4199 1067 30 124 O

ATOM 1678 N ILE A 525 -22.026 24.558 -20.195 1.00 24.87 N

ANISOU 1678 N ILE A 525 5049 2880 1522 999 -118 99 N

ATOM 1679 CA ILE A 525 -22.252 23.174 -20.622 1.00 23.93 C

ANISOU 1679 CA ILE A 525 4992 2738 1362 1010 -173 70 C

ATOM 1680 CB ILE A 525 -23.028 22.344 -19.565 1.00 25.67 C

ANISOU 1680 CB ILE A 525 5133 2976 1644 959 -248 45 C

ATOM 1681 CG2 ILE A 525 -22.270 22.329 -18.253 1.00 27.22 C ANISOU 1681 CG2 ILE A 525 5223 3204 1917 924 -187 52 C

ATOM 1682 CGI ILE A 525 -24.446 22.882 -19.371 1.00 29.35 C

ANISOU 1682 CGI ILE A 525 5564 3449 2137 933 -337 42 C

ATOM 1683 CD 1 ILE A 525 -25.539 21.932 -19.814 1.00 33.03 C

ANISOU 1683 CD 1 ILE A 525 6077 3893 2578 930 -447 12 C

ATOM 1684 C ILE A 525 -22.908 23.053 -22.002 1.00 34.38 C

ANISOU 1684 C ILE A 525 6439 4026 2599 1052 -233 62 C

ATOM 1685 0 ILE A 525 -22.832 22.004 -22.647 1.00 28.28 O

ANISOU 1685 O ILE A 525 5748 3227 1772 1075 -258 42 O

ATOM 1686 N ASN A 526 -23.537 24.130 -22.460 1.00 29.58 N

ANISOU 1686 N ASN A 526 5849 3415 1974 1063 -256 77 N

ATOM 1687 CA ASN A 526 -24.189 24.121 -23.765 1.00 35.92 C

ANISOU 1687 CA ASN A 526 6770 4184 2694 1104 -317 70 C

ATOM 1688 CB ASN A 526 -24.997 25.405 -23.981 1.00 46.53 C

ANISOU 1688 CB ASN A 526 8105 5533 4041 1107 -348 88 C

ATOM 1689 CG ASN A 526 -26.277 25.431 -23.170 1.00 63.03 C

ANISOU 1689 CG ASN A 526 10107 7644 6198 1059 -443 75 C

ATOM 1690 OD1 ASN A 526 -26.770 24.389 -22.731 1.00 57.84 O

ANISOU 1690 OD1 ASN A 526 9422 6989 5567 1031 -507 48 O

ATOM 1691 ND2 ASN A 526 -26.826 26.624 -22.968 1.00 73.17 N ANISOU 1691 ND2 ASN A 526 11347 8943 7511 1051 -450 95 N

ATOM 1692 C ASN A 526 -23.199 23.911 -24.909 1.00 40.64 C

ANISOU 1692 C ASN A 526 7488 4749 3206 1163 -248 77 C

ATOM 1693 0 ASN A 526 -23.552 23.352 -25.946 1.00 47.97 O

ANISOU 1693 0 ASN A 526 8528 5642 4057 1198 -299 62 O

ATOM 1694 N VAL A 527 -21.959 24.352 -24.707 1.00 32.53 N

ANISOU 1694 N VAL A 527 6438 3730 2192 1173 -131 101 N

ATOM 1695 C A VAL A 527 -20.912 24.223 -25.716 1.00 39.31 C

ANISOU 1695 CA VAL A 527 7401 4558 2978 1228 -49 112 C

ATOM 1696 CB VAL A 527 -19.750 25.199 -25.450 1.00 52.99 C

ANISOU 1696 CB VAL A 527 9088 6304 4740 1233 77 146 C

ATOM 1697 CGI VAL A 527 -20.289 26.592 -25.167 1.00 54.77 C

ANISOU 1697 CGI VAL A 527 9261 6548 5000 1215 72 167 C

ATOM 1698 CG2 VAL A 527 -18.897 24.709 -24.293 1.00 54.06 C ANISOU 1698 CG2 VAL A 527 9119 6469 4953 1197 132 144 C

ATOM 1699 C VAL A 527 -20.355 22.804 -25.806 1.00 44.08 C

ANISOU 1699 C VAL A 527 8043 5146 3559 1238 -41 91 C

ATOM 1700 O VAL A 527 -19.569 22.491 -26.704 1.00 39.37 O

ANISOU 1700 O VAL A 527 7545 4519 2896 1287 18 96 O

ATOM 1701 N LEU A 528 -20.754 21.948 -24.869 1.00 36.16 N

ANISOU 1701 N LEU A 528 6966 4163 2612 1194 -98 67 N

ATOM 1702 CA LEU A 528 -20.416 20.530 -24.945 1.00 37.08 C

ANISOU 1702 CA LEU A 528 7121 4263 2705 1201 -107 43 C

ATOM 1703 CB LEU A 528 -20.528 19.876 -23.566 1.00 39.20 C

ANISOU 1703 CB LEU A 528 7270 4563 3060 1145 -132 28 C

ATOM 1704 CG LEU A 528 -19.542 20.360 -22.508 1.00 33.12 C ANISOU 1704 CG LEU A 528 6390 3829 2366 1121 -39 49 C ATOM 1705 CD 1 LEU A 528 -19.960 19.887 -21.112 1.00 32.60 C ANISOU 1705 CD 1 LEU A 528 6208 3795 2385 1062 -83 33 C ATOM 1706 CD2 LEU A 528 -18.132 19.892 -22.849 1.00 46.37 C ANISOU 1706 CD2 LEU A 528 8109 5494 4017 1159 62 58 C

ATOM 1707 C LEU A 528 -21.354 19.830 -25.919 1.00 34.55 C

ANISOU 1707 C LEU A 528 6912 3906 2311 1223 -208 17 C

ATOM 1708 O LEU A 528 -21.095 18.709 -26.353 1.00 35.11 O

ANISOU 1708 O LEU A 528 7054 3950 2335 1243 -216 -3 O

ATOM 1709 N HIS A 529 -22.454 20.501 -26.248 1.00 33.66 N

ANISOU 1709 N HIS A 529 6812 3790 2186 1219 -286 16 N

ATOM 1710 CA HIS A 529 -23.457 19.954 -27.158 1.00 41.41 C

ANISOU 1710 CA HIS A 529 7893 4738 3103 1236 -393 -9 C

ATOM 1711 CB HIS A 529 -22.981 20.069 -28.610 1.00 40.38 C

ANISOU 1711 CB HIS A 529 7915 4564 2863 1305 -357 -0 C

ATOM 1712 CG HIS A 529 -22.724 21.480 -29.037 1.00 45.54 C

ANISOU 1712 CG HIS A 529 8584 5220 3498 1332 -297 34 C ATOM 1713 CD2 HIS A 529 -23.575 22.499 -29.302 1.00 40.67 C ANISOU 1713 CD2 HIS A 529 7969 4607 2877 1333 -347 45 C ATOM 1714 ND1 HIS A 529 -21.454 21.994 -29.187 1.00 51.43 N ANISOU 1714 ND1 HIS A 529 9341 5965 4235 1361 -166 63 N ATOM 1715 CE1 HIS A 529 -21.533 23.263 -29.546 1.00 54.07 C ANISOU 1715 CE1 HIS A 529 9686 6300 4557 1378 -138 89 C ATOM 1716 NE2 HIS A 529 -22.810 23.595 -29.622 1.00 52.30 N ANISOU 1716 NE2 HIS A 529 9459 6079 4334 1363 -246 79 N

ATOM 1717 C HIS A 529 -23.844 18.519 -26.811 1.00 38.69 C

ANISOU 1717 C HIS A 529 7542 4385 2772 1210 -463 -44 C

ATOM 1718 O HIS A 529 -24.055 17.687 -27.695 1.00 40.83 O

ANISOU 1718 0 HIS A 529 7924 4618 2972 1238 -512 -66 O

ATOM 1719 N LYS A 530 -23.939 18.240 -25.515 1.00 41.74 N

ANISOU 1719 N LYS A 530 7803 4805 3250 1156 -468 -50 N ATOM 1720 CA LYS A 530 -24.387 16.934 -25.047 1.00 38.39 C ANISOU 1720 CA LYS A 530 7360 4375 2849 1124 -535 -83 C ATOM 1721 CB LYS A 530 -23.943 16.687 -23.601 1.00 44.80 C ANISOU 1721 CB LYS A 530 8043 5226 3755 1078 -491 -80 C ATOM 1722 CG LYS A 530 -22.446 16.511 -23.416 1.00 42.08 C ANISOU 1722 CG LYS A 530 7695 4886 3407 1100 -371 -64 C ATOM 1723 CD LYS A 530 -22.117 16.108 -21.985 1.00 36.88 C ANISOU 1723 CD LYS A 530 6915 4262 2837 1053 -346 -67 C ATOM 1724 CE LYS A 530 -22.111 14.599 -21.814 1.00 36.48 C ANISOU 1724 CE LYS A 530 6887 4192 2779 1045 -379 -96 C ATOM 1725 NZ LYS A 530 -20.875 13.983 -22.375 1.00 34.61 N ANISOU 1725 NZ LYS A 530 6726 3935 2489 1091 -299 -92 N

ATOM 1726 C LYS A 530 -25.902 16.827 -25.132 1.00 34.80 C ANISOU 1726 C LYS A 530 6901 3914 2406 1097 -667 -105 C

ATOM 1727 O LYS A 530 -26.620 17.768 -24.791 1.00 36.88 O ANISOU 1727 0 LYS A 530 7100 4201 2712 1075 -699 -93 O

ATOM 1728 N PRO A 531 -26.393 15.672 -25.593 1.00 33.76 N

ANISOU 1728 N PRO A 531 6838 3751 2237 1099 -744 -137 N

ATOM 1729 CD PRO A 531 -25.606 14.543 -26.116 1.00 41.14 C

ANISOU 1729 CD PRO A 531 7865 4654 3111 1129 -711 -152 C

ATOM 1730 CA PRO A 531 -27.826 15.381 -25.564 1.00 37.55 C

ANISOU 1730 CA PRO A 531 7303 4225 2738 1066 -874 -161 C

ATOM 1731 CB PRO A 531 -27.918 14.040 -26.293 1.00 47.65 C

ANISOU 1731 CB PRO A 531 8691 5462 3954 1082 -928 -194 C

ATOM 1732 CG PRO A 531 -26.584 13.406 -26.072 1.00 50.94 C

ANISOU 1732 CG PRO A 531 9122 5876 4359 1100 -824 -189 C

ATOM 1733 C PRO A 531 -28.295 15.209 -24.124 1.00 42.27 C

ANISOU 1733 C PRO A 531 7758 4860 3445 1001 -893 -166 C

ATOM 1734 O PRO A 531 -27.475 14.964 -23.238 1.00 32.04 O

ANISOU 1734 0 PRO A 531 6395 3584 2193 984 -817 -158 O

ATOM 1735 N PRO A 532 -29.604 15.351 -23.886 1.00 43.17 N

ANISOU 1735 N PRO A 532 7823 4979 3600 965 -994 -177 N

ATOM 1736 CD PRO A 532 -30.636 15.856 -24.804 1.00 37.15 C

ANISOU 1736 CD PRO A 532 7117 4199 2799 982 -1087 -182 C

ATOM 1737 CA PRO A 532 -30.139 15.056 -22.555 1.00 38.37 C

ANISOU 1737 CA PRO A 532 7088 4400 3092 904 -1018 -185 C

ATOM 1738 CB PRO A 532 -31.633 15.370 -22.692 1.00 38.99 C

ANISOU 1738 CB PRO A 532 7140 4475 3199 880 -1134 -195 C

ATOM 1739 CG PRO A 532 -31.902 15.390 -24.165 1.00 44.37 C

ANISOU 1739 CG PRO A 532 7954 5119 3785 928 -1190 -204 C

ATOM 1740 C PRO A 532 -29.936 13.587 -22.221 1.00 34.97 C

ANISOU 1740 C PRO A 532 6668 3952 2666 885 -1030 -213 C

ATOM 1741 O PRO A 532 -29.931 12.742 -23.115 1.00 30.66 O

ANISOU 1741 O PRO A 532 6228 3369 2052 910 -1069 -235 O

ATOM 1742 N TYR A 533 -29.767 13.290 -20.940 1.00 24.75 N

ANISOU 1742 N TYR A 533 5269 2685 1451 842 -997 -212 N

ATOM 1743 CA TYR A 533 -29.552 11.918 -20.498 1.00 29.83 C

ANISOU 1743 CA TYR A 533 5915 3314 2106 822 -1002 -236 C

ATOM 1744 CB TYR A 533 -28.850 11.906 -19.139 1.00 24.79 C

ANISOU 1744 CB TYR A 533 5170 2709 1539 793 -922 -222 C

ATOM 1745 CG TYR A 533 -27.409 12.373 -19.151 1.00 27.03 C

ANISOU 1745 CG TYR A 533 5464 3007 1800 829 -804 -197 C

ATOM 1746 CD 1 TYR A 533 -26.371 11.490 -19.443 1.00 27.03 C

ANISOU 1746 CD 1 TYR A 533 5528 2988 1755 859 -750 -204 C

ATOM 1747 CE1 TYR A 533 -25.052 11.909 -19.440 1.00 25.71 C

ANISOU 1747 CE1 TYR A 533 5364 2834 1573 891 -642 -180 C

ATOM 1748 CD2 TYR A 533 -27.086 13.691 -18.851 1.00 20.17 C

ANISOU 1748 CD2 TYR A 533 4538 2169 957 833 -746 -166 C

ATOM 1749 CE2 TYR A 533 -25.774 14.117 -18.843 1.00 29.66 C

ANISOU 1749 CE2 TYR A 533 5744 3382 2144 863 -640 -143 C

ATOM 1750 CZ TYR A 533 -24.760 13.224 -19.135 1.00 27.14 C ANISOU 1750 CZ TYR A 533 5484 3045 1783 892 -588 -150 C

ATOM 1751 OH TYR A 533 -23.451 13.657 -19.131 1.00 27.82 O

ANISOU 1751 OH TYR A 533 5569 3144 1858 921 -482 -126 O

ATOM 1752 C TYR A 533 -30.860 11.150 -20.360 1.00 30.81 C

ANISOU 1752 C TYR A 533 6022 3421 2263 780 -1117 -266 C

ATOM 1753 O TYR A 533 -31.880 11.705 -19.932 1.00 27.90 O

ANISOU 1753 0 TYR A 533 5578 3068 1954 747 -1172 -263 O

ATOM 1754 N GLU A 534 -30.823 9.864 -20.704 1.00 23.60 N

ANISOU 1754 N GLU A 534 5178 2475 1315 782 -1151 -295 N

ATOM 1755 CA GLU A 534 -31.933 8.970 -20.406 1.00 31.40 C

ANISOU 1755 CA GLU A 534 6140 3444 2344 736 -1248 -324 C

ATOM 1756 CB GLU A 534 -31.867 7.712 -21.282 1.00 36.64 C

ANISOU 1756 CB GLU A 534 6924 4062 2937 755 -1293 -356 C

ATOM 1757 CG GLU A 534 -32.181 7.954 -22.751 1.00 50.83 C

ANISOU 1757 CG GLU A 534 8841 5826 4646 798 -1352 -364 C

ATOM 1758 CD GLU A 534 -32.161 6.672 -23.567 1.00 65.68 C ANISOU 1758 CD GLU A 534 10842 7658 6458 814 -1401 -398 C

ATOM 1759 OEl GLU A 534 -31.512 5.697 -23.129 1.00 67.64 O ANISOU 1759 OEl GLU A 534 11096 7897 6707 808 -1356 -408 O

ATOM 1760 OE2 GLU A 534 -32.790 6.640 -24.647 1.00 70.76 O ANISOU 1760 OE2 GLU A 534 11574 8269 7043 833 -1485 -414 O

ATOM 1761 C GLU A 534 -31.866 8.582 -18.934 1.00 27.48 C

ANISOU 1761 C GLU A 534 5530 2973 1937 687 -1212 -323 C

ATOM 1762 0 GLU A 534 -30.856 8.058 -18.471 1.00 30.86 O

ANISOU 1762 0 GLU A 534 5958 3407 2362 695 -1137 -320 O

ATOM 1763 N HIS A 535 -32.939 8.843 -18.199 1.00 27.24 N

ANISOU 1763 N HIS A 535 5403 2957 1988 639 -1266 -324 N

ATOM 1764 CA HIS A 535 -32.948 8.603 -16.761 1.00 28.13 C

ANISOU 1764 CA HIS A 535 5406 3094 2188 593 -1231 -320 C

ATOM 1765 CB HIS A 535 -33.618 9.770 -16.027 1.00 22.63 C

ANISOU 1765 CB HIS A 535 4600 2431 1566 565 -1233 -297 C

ATOM 1766 CG HIS A 535 -32.889 11.072 -16.159 1.00 21.28 C

ANISOU 1766 CG HIS A 535 4421 2289 1375 599 -1160 -264 C

ATOM 1767 CD2 HIS A 535 -31.579 11.381 -16.008 1.00 25.42 C

ANISOU 1767 CD2 HIS A 535 4956 2830 1873 627 -1059 -245 C

ATOM 1768 ND1 HIS A 535 -33.523 12.251 -16.489 1.00 27.78 N

ANISOU 1768 ND1 HIS A 535 5223 3125 2206 605 -1188 -248 N

ATOM 1769 CE1 HIS A 535 -32.636 13.229 -16.533 1.00 26.42 C

ANISOU 1769 CE1 HIS A 535 5051 2975 2012 635 -1106 -220 C

ATOM 1770 NE2 HIS A 535 -31.449 12.728 -16.244 1.00 22.12 N

ANISOU 1770 NE2 HIS A 535 4523 2434 1448 648 -1027 -218 N

ATOM 1771 C HIS A 535 -33.676 7.302 -16.438 1.00 31.57 C

ANISOU 1771 C HIS A 535 5836 3502 2656 552 -1298 -351 C

ATOM 1772 0 HIS A 535 -34.613 6.925 -17.141 1.00 30.82 O

ANISOU 1772 0 HIS A 535 5784 3379 2549 544 -1394 -374 O

ATOM 1773 N PRO A 536 -33.248 6.611 -15.372 1.00 27.29 N ANISOU 1773 N PRO A 536 5243 2967 2158 526 -1250 -354 N

ATOM 1774 CD PRO A 536 -32.121 6.945 -14.483 1.00 27.79 C

ANISOU 1774 CD PRO A 536 5256 3062 2239 534 -1143 -330 C

ATOM 1775 CA PRO A 536 -33.963 5.406 -14.941 1.00 28.70 C

ANISOU 1775 CA PRO A 536 5408 3120 2376 483 -1308 -382 C

ATOM 1776 CB PRO A 536 -33.218 4.982 -13.665 1.00 25.86 C

ANISOU 1776 CB PRO A 536 4986 2778 2060 465 -1227 -374 C

ATOM 1777 CG PRO A 536 -32.448 6.190 -13.233 1.00 33.36 C

ANISOU 1777 CG PRO A 536 5886 3770 3020 485 -1143 -339 C

ATOM 1778 C PRO A 536 -35.415 5.748 -14.627 1.00 31.25 C

ANISOU 1778 C PRO A 536 5655 3445 2774 437 -1389 -386 C

ATOM 1779 0 PRO A 536 -35.685 6.863 -14.185 1.00 28.63 O

ANISOU 1779 0 PRO A 536 5248 3144 2486 430 -1371 -362 O

ATOM 1780 N LYS A 537 -36.329 4.809 -14.852 1.00 29.85 N

ANISOU 1780 N LYS A 537 5497 3233 2612 407 -1475 -416 N

ATOM 1781 CA LYS A 537 -37.752 5.054 -14.623 1.00 38.32 C

ANISOU 1781 CA LYS A 537 6498 4304 3759 364 -1558 -422 C

ATOM 1782 CB LYS A 537 -38.559 4.782 -15.895 1.00 55.33 C

ANISOU 1782 CB LYS A 537 8730 6422 5870 372 -1667 -446 C

ATOM 1783 CG LYS A 537 -38.256 5.721 -17.048 1.00 73.68 C

ANISOU 1783 CG LYS A 537 11126 8752 8116 426 -1674 -434 C

ATOM 1784 CD LYS A 537 -39.153 5.411 -18.238 1.00 89.27 C ANISOU 1784 CD LYS A 537 13176 10689 10053 431 -1792 -460 C

ATOM 1785 CE LYS A 537 -38.937 6.387 -19.384 1.00 91.87 C

ANISOU 1785 CE LYS A 537 13579 11022 10305 486 -1803 -447 C

ATOM 1786 NZ LYS A 537 -39.818 6.068 -20.543 1.00 85.96 N ANISOU 1786 NZ LYS A 537 12908 10236 9517 492 -1924 -474 N

ATOM 1787 C LYS A 537 -38.296 4.204 -13.481 1.00 32.31 C

ANISOU 1787 C LYS A 537 5661 3534 3082 307 -1564 -433 C

ATOM 1788 O LYS A 537 -39.467 4.307 -13.116 1.00 35.57 O

ANISOU 1788 0 LYS A 537 6002 3944 3569 265 -1623 -437 O

ATOM 1789 N ASP A 538 -37.437 3.364 -12.917 1.00 28.17 N

ANISOU 1789 N ASP A 538 5153 3005 2546 307 -1502 -438 N

ATOM 1790 CA ASP A 538 -37.819 2.507 -11.808 1.00 22.93 C

ANISOU 1790 CA ASP A 538 4427 2331 1955 257 -1497 -448 C

ATOM 1791 CB ASP A 538 -38.562 1.269 -12.320 1.00 33.31 C

ANISOU 1791 CB ASP A 538 5793 3597 3267 232 -1584 -485 C

ATOM 1792 CG ASP A 538 -37.823 0.563 -13.447 1.00 43.37 C

ANISOU 1792 CG ASP A 538 7198 4841 4437 274 -1594 -505 C

ATOM 1793 ODl ASP A 538 -38.441 0.354 -14.514 1.00 40.60 O

ANISOU 1793 ODl ASP A 538 6913 4462 4052 279 -1681 -526 O

ATOM 1794 OD2 ASP A 538 -36.630 0.220 -13.276 1.00 33.05 O

ANISOU 1794 OD2 ASP A 538 5932 3540 3086 304 -1515 -499 O

ATOM 1795 C ASP A 538 -36.570 2.099 -11.055 1.00 23.07 C

ANISOU 1795 C ASP A 538 4448 2361 1957 272 -1398 -439 C

ATOM 1796 O ASP A 538 -35.484 2.594 -11.345 1.00 31.83 O ANISOU 1796 0 ASP A 538 5594 3490 3009 317 -1334 -422 O

ATOM 1797 N LEU A 539 -36.716 1.178 -10.109 1.00 27.26 N

ANISOU 1797 N LEU A 539 4943 2878 2537 235 -1385 -449 N

ATOM 1798 CA LEU A 539 -35.592 0.762 -9.274 1.00 23.82 C

ANISOU 1798 CA LEU A 539 4503 2454 2094 246 -1295 -440 C

ATOM 1799 CB LEU A 539 -35.947 0.930 -7.792 1.00 27.50 C

ANISOU 1799 CB LEU A 539 4860 2939 2651 204 -1259 -425 C

ATOM 1800 CG LEU A 539 -36.562 2.271 -7.367 1.00 28.63 C

ANISOU 1800 CG LEU A 539 4912 3115 2850 190 -1258 -400 C

ATOM 1801 CDl LEU A 539 -36.866 2.279 -5.878 1.00 26.68 C

ANISOU 1801 CDl LEU A 539 4569 2879 2688 149 -1218 -388 C

ATOM 1802 CD2 LEU A 539 -35.659 3.433 -7.729 1.00 14.63 C

ANISOU 1802 CD2 LEU A 539 3150 1378 1031 235 -1205 -375 C

ATOM 1803 C LEU A 539 -35.137 -0.680 -9.553 1.00 32.33 C

ANISOU 1803 C LEU A 539 5664 3493 3127 253 -1299 -467 C

ATOM 1804 O LEU A 539 -34.419 -1.280 -8.749 1.00 30.46 O

ANISOU 1804 O LEU A 539 5419 3259 2897 253 -1238 -464 O

ATOM 1805 N LYS A 540 -35.532 -1.224 -10.702 1.00 35.16 N

ANISOU 1805 N LYS A 540 6107 3816 3436 262 -1372 -492 N

ATOM 1806 CA LYS A 540 -35.255 -2.629 -11.015 1.00 31.18 C

ANISOU 1806 CA LYS A 540 5686 3270 2891 264 -1386 -520 C

ATOM 1807 CB LYS A 540 -36.073 -3.086 -12.228 1.00 40.77 C

ANISOU 1807 CB LYS A 540 6977 4443 4070 260 -1488 -550 C

ATOM 1808 CG LYS A 540 -37.578 -2.998 -12.016 1.00 43.94 C

ANISOU 1808 CG LYS A 540 7310 4835 4552 204 -1574 -561 C

ATOM 1809 CD LYS A 540 -38.345 -3.598 -13.182 1.00 58.18 C

ANISOU 1809 CD LYS A 540 9192 6593 6321 197 -1680 -594 C

ATOM 1810 CE LYS A 540 -39.849 -3.510 -12.961 1.00 66.10 C

ANISOU 1810 CE LYS A 540 10119 7586 7412 140 -1767 -604 C

ATOM 1811 NZ LYS A 540 -40.326 -2.098 -12.881 1.00 73.37 N

ANISOU 1811 NZ LYS A 540 10961 8546 8371 142 -1773 -578 N

ATOM 1812 C LYS A 540 -33.772 -2.935 -11.222 1.00 27.72 C

ANISOU 1812 C LYS A 540 5318 2836 2378 317 -1306 -514 C

ATOM 1813 0 LYS A 540 -33.262 -3.932 -10.712 1.00 38.46 O

ANISOU 1813 0 LYS A 540 6697 4179 3736 315 -1271 -523 O

ATOM 1814 N LEU A 541 -33.081 -2.077 -11.962 1.00 26.14 N

ANISOU 1814 N LEU A 541 5156 2657 2121 366 -1276 -497 N

ATOM 1815 CA LEU A 541 -31.658 -2.270 -12.220 1.00 34.15 C

ANISOU 1815 CA LEU A 541 6232 3676 3067 419 -1197 -488 C

ATOM 1816 CB LEU A 541 -31.190 -1.360 -13.358 1.00 41.61 C

ANISOU 1816 CB LEU A 541 7236 4632 3942 470 -1187 -475 C

ATOM 1817 CG LEU A 541 -31.915 -1.566 -14.689 1.00 50.39 C

ANISOU 1817 CG LEU A 541 8439 5707 5000 479 -1277 -499 C

ATOM 1818 CDl LEU A 541 -31.376 -0.622 -15.753 1.00 55.38 C

ANISOU 1818 CDl LEU A 541 9131 6350 5561 533 -1257 -483 C

ATOM 1819 CD2 LEU A 541 -31.788 -3.015 -15.136 1.00 49.68 C ANISOU 1819 CD2 LEU A 541 8445 5568 4864 483 -1303 -530 C ATOM 1820 C LEU A 541 -30.804 -2.040 -10.977 1.00 33.49 C ANISOU 1820 C LEU A 541 6072 3628 3024 419 -1104 -463 C ATOM 1821 0 LEU A 541 -29.632 -2.405 -10.944 1.00 31.82 O ANISOU 1821 O LEU A 541 5899 3420 2773 456 -1037 -457 O ATOM 1822 N SER A 542 -31.391 -1.431 -9.952 1.00 30.27 N ANISOU 1822 N SER A 542 5557 3246 2696 379 -1102 -449 N ATOM 1823 CA SER A 542 -30.668 -1.215 -8.703 1.00 26.48 C ANISOU 1823 CA SER A 542 5005 2799 2258 376 -1022 -428 C ATOM 1824 CB SER A 542 -30.716 0.260 -8.279 1.00 30.09 C ANISOU 1824 CB SER A 542 5379 3300 2753 373 -994 -398 C ATOM 1825 OG SER A 542 -32.018 0.802 -8.421 1.00 24.15 O ANISOU 1825 OG SER A 542 4587 2547 2044 339 -1064 -401 O ATOM 1826 C SER A 542 -31.196 -2.116 -7.595 1.00 26.52 C ANISOU 1826 C SER A 542 4963 2787 2326 329 -1032 -439 C ATOM 1827 O SER A 542 -30.989 -1.844 -6.417 1.00 21.85 O ANISOU 1827 0 SER A 542 4295 2220 1786 313 -984 -423 O ATOM 1828 N ASP A 543 -31.879 -3.190 -7.980 1.00 27.28 N ANISOU 1828 N ASP A 543 5109 2840 2416 308 -1094 -469 N ATOM 1829 CA ASP A 543 -32.347 -4.179 -7.013 1.00 26.98 C ANISOU 1829 CA ASP A 543 5040 2779 2432 265 -1101 -482 C ATOM 1830 CB ASP A 543 -31.150 -4.845 -6.329 1.00 40.18 C ANISOU 1830 CB ASP A 543 6728 4454 4086 289 -1023 -476 C ATOM 1831 CG ASP A 543 -31.547 -6.029 -5.469 1.00 60.10 C ANISOU 1831 CG ASP A 543 9240 6945 6649 251 -1030 -492 C ATOM 1832 ODl ASP A 543 -30.696 -6.495 -4.682 1.00 63.42 O ANISOU 1832 ODl ASP A 543 9656 7372 7069 265 -967 -485 O ATOM 1833 OD2 ASP A 543 -32.705 -6.493 -5.576 1.00 66.24 O ANISOU 1833 OD2 ASP A 543 10014 7692 7461 208 -1098 -512 O ATOM 1834 C ASP A 543 -33.283 -3.556 -5.971 1.00 22.19 C ANISOU 1834 C ASP A 543 4323 2191 1917 215 -1110 -469 C ATOM 1835 O ASP A 543 -33.240 -3.905 -4.789 1.00 25.76 O ANISOU 1835 0 ASP A 543 4724 2646 2419 192 -1072 -463 O ATOM 1836 N GLY A 544 -34.123 -2.628 -6.418 1.00 23.64 N ANISOU 1836 N GLY A 544 4473 2387 2122 203 -1158 -464 N ATOM 1837 CA GLY A 544 -35.110 -2.011 -5.555 1.00 21.20 C ANISOU 1837 CA GLY A 544 4062 2092 1900 158 -1172 -452 C ATOM 1838 C GLY A 544 -34.558 -0.894 -4.681 1.00 26.96 C ANISOU 1838 C GLY A 544 4719 2868 2656 168 -1100 -419 C ATOM 1839 O GLY A 544 -35.283 -0.340 -3.853 1.00 21.93 O ANISOU 1839 0 GLY A 544 3997 2244 2090 134 -1100 -406 O ATOM 1840 N ARG A 545 -33.279 -0.562 -4.858 1.00 18.26 N ANISOU 1840 N ARG A 545 3649 1790 1499 215 -1039 -405 N ATOM 1841 CA ARG A 545 -32.651 0.483 -4.054 1.00 17.07 C ANISOU 1841 CA ARG A 545 3434 1682 1370 226 -970 -375 C ATOM 1842 CB ARG A 545 -31.201 0.119 -3.729 1.00 16.74 C ANISOU 1842 CB ARG A 545 3422 1651 1287 262 -895 -368 C

ATOM 1843 CG ARG A 545 -31.043 -1.136 -2.873 1.00 21.16 C

ANISOU 1843 CG ARG A 545 3987 2187 1865 245 -878 -381 C

ATOM 1844 CD ARG A 545 -29.790 -1.030 -2.019 1.00 36.64 C

ANISOU 1844 CD ARG A 545 5928 4173 3821 270 -797 -363 C

ATOM 1845 NE ARG A 545 -28.631 -1.605 -2.679 1.00 38.27 N

ANISOU 1845 NE ARG A 545 6210 4374 3958 317 -767 -368 N

ATOM 1846 CZ ARG A 545 -27.370 -1.402 -2.306 1.00 30.64 C

ANISOU 1846 CZ ARG A 545 5238 3431 2972 352 -699 -352 C

ATOM 1847 NHl ARG A 545 -27.070 -0.610 -1.277 1.00 22.20 N ANISOU 1847 NHl ARG A 545 4094 2395 1945 344 -656 -330 N

ATOM 1848 NH2 ARG A 545 -26.402 -1.985 -2.985 1.00 24.19 N ANISOU 1848 NH2 ARG A 545 4492 2605 2094 395 -675 -357 N

ATOM 1849 C ARG A 545 -32.671 1.818 -4.782 1.00 17.31 C

ANISOU 1849 C ARG A 545 3456 1740 1381 248 -976 -358 C

ATOM 1850 O ARG A 545 -32.489 1.862 -6.001 1.00 18.94 O

ANISOU 1850 O ARG A 545 3733 1937 1526 279 -1003 -366 O

ATOM 1851 N LEU A 546 -32.884 2.899 -4.035 1.00 21.19 N

ANISOU 1851 N LEU A 546 3866 2263 1922 234 -950 -334 N

ATOM 1852 CA LEU A 546 -32.776 4.246 -4.594 1.00 16.02 C

ANISOU 1852 CA LEU A 546 3200 1637 1251 257 -943 -315 C

ATOM 1853 CB LEU A 546 -33.653 5.238 -3.822 1.00 20.45 C

ANISOU 1853 CB LEU A 546 3668 2218 1884 223 -948 -297 C

ATOM 1854 CG LEU A 546 -33.859 6.635 -4.426 1.00 22.35 C

ANISOU 1854 CG LEU A 546 3893 2483 2117 240 -956 -278 C

ATOM 1855 CDl LEU A 546 -34.749 6.595 -5.677 1.00 15.47 C ANISOU 1855 CDl LEU A 546 3066 1590 1222 244 -1040 -293 C

ATOM 1856 CD2 LEU A 546 -34.456 7.577 -3.389 1.00 22.47 C

ANISOU 1856 CD2 LEU A 546 3812 2520 2205 211 -937 -257 C

ATOM 1857 C LEU A 546 -31.322 4.688 -4.546 1.00 17.25 C

ANISOU 1857 C LEU A 546 3372 1819 1363 298 -865 -297 C

ATOM 1858 O LEU A 546 -30.699 4.706 -3.477 1.00 19.46 O

ANISOU 1858 0 LEU A 546 3609 2116 1670 294 -807 -285 O

ATOM 1859 N ARG A 547 -30.780 5.039 -5.707 1.00 17.06 N

ANISOU 1859 N ARG A 547 3411 1797 1274 340 -863 -295 N

ATOM 1860 CA ARG A 547 -29.397 5.481 -5.800 1.00 15.63 C

ANISOU 1860 CA ARG A 547 3248 1640 1053 381 -789 -278 C

ATOM 1861 CB ARG A 547 -28.797 5.104 -7.166 1.00 17.48 C

ANISOU 1861 CB ARG A 547 3584 1855 1203 427 -794 -288 C

ATOM 1862 CG ARG A 547 -28.601 3.597 -7.333 1.00 18.13 C

ANISOU 1862 CG ARG A 547 3729 1902 1256 431 -809 -313 C

ATOM 1863 CD ARG A 547 -28.024 3.197 -8.694 1.00 14.25 C

ANISOU 1863 CD ARG A 547 3345 1389 679 478 -812 -324 C

ATOM 1864 NE ARG A 547 -27.487 1.836 -8.641 1.00 23.83 N

ANISOU 1864 NE ARG A 547 4612 2576 1866 488 -800 -342 N

ATOM 1865 CZ ARG A 547 -27.437 1.003 -9.679 1.00 23.34 C ANISOU 1865 CZ ARG A 547 4649 2478 1742 511 -830 -363 C

ATOM 1866 NHl ARG A 547 -27.904 1.378 -10.856 1.00 20.07 N

ANISOU 1866 NHl ARG A 547 4292 2050 1283 527 -878 -369 N

ATOM 1867 NH2 ARG A 547 -26.929 -0.209 -9.532 1.00 17.67 N

ANISOU 1867 NH2 ARG A 547 3975 1737 1004 521 -814 -378 N

ATOM 1868 C ARG A 547 -29.320 6.983 -5.543 1.00 18.50 C

ANISOU 1868 C ARG A 547 3552 2039 1439 383 -757 -250 C

ATOM 1869 0 ARG A 547 -29.851 7.780 -6.314 1.00 19.26 O

ANISOU 1869 0 ARG A 547 3658 2138 1523 390 -789 -244 O

ATOM 1870 N VAL A 548 -28.685 7.361 -4.435 1.00 11.47 N

ANISOU 1870 N VAL A 548 2600 1173 584 377 -696 -233 N

ATOM 1871 CA VAL A 548 -28.557 8.773 -4.072 1.00 11.77 C

ANISOU 1871 CA VAL A 548 2580 1245 648 376 -662 -207 C

ATOM 1872 CB VAL A 548 -29.062 9.036 -2.637 1.00 16.40 C

ANISOU 1872 CB VAL A 548 3079 1843 1309 334 -651 -198 C

ATOM 1873 CGI VAL A 548 -28.937 10.529 -2.279 1.00 13.37 C

ANISOU 1873 CGI VAL A 548 2638 1491 949 334 -616 -172 C

ATOM 1874 CG2 VAL A 548 -30.501 8.571 -2.502 1.00 15.78 C

ANISOU 1874 CG2 VAL A 548 2982 1743 1272 296 -719 -213 C

ATOM 1875 C VAL A 548 -27.100 9.203 -4.191 1.00 11.90 C

ANISOU 1875 C VAL A 548 2611 1282 629 414 -588 -191 C

ATOM 1876 O VAL A 548 -26.217 8.555 -3.637 1.00 15.23 O

ANISOU 1876 0 VAL A 548 3033 1705 1048 423 -547 -193 O

ATOM 1877 N GLY A 549 -26.852 10.277 -4.939 1.00 15.06 N

ANISOU 1877 N GLY A 549 3024 1696 1003 439 -572 -175 N

ATOM 1878 CA GLY A 549 -25.510 10.804 -5.085 1.00 17.72 C

ANISOU 1878 CA GLY A 549 3367 2051 1314 473 -500 -157 C

ATOM 1879 C GLY A 549 -25.343 12.126 -4.346 1.00 14.15 C

ANISOU 1879 C GLY A 549 2842 1631 904 460 -461 -133 C

ATOM 1880 O GLY A 549 -26.039 13.096 -4.640 1.00 15.44 O

ANISOU 1880 O GLY A 549 2989 1802 1075 453 -482 -123 O

ATOM 1881 N TYR A 550 -24.422 12.157 -3.387 1.00 13.79 N

ANISOU 1881 N TYR A 550 2752 1602 885 458 -405 -123 N

ATOM 1882 CA TYR A 550 -24.068 13.384 -2.679 1.00 11.32 C

ANISOU 1882 CA TYR A 550 2375 1318 608 449 -362 -101 C

ATOM 1883 CB TYR A 550 -23.774 13.072 -1.206 1.00 9.81 C

ANISOU 1883 CB TYR A 550 2124 1137 466 423 -339 -100 C

ATOM 1884 CG TYR A 550 -24.988 12.628 -0.414 1.00 11.89 C

ANISOU 1884 CG TYR A 550 2357 1391 770 383 -387 -111 C

ATOM 1885 CD1 TYR A 550 -25.949 13.542 -0.026 1.00 12.23 C

ANISOU 1885 CD 1 TYR A 550 2353 1442 853 355 -407 -101 C

ATOM 1886 CE1 TYR A 550 -27.059 13.153 0.708 1.00 13.23 C

ANISOU 1886 CE1 TYR A 550 2447 1556 1024 318 -444 -110 C

ATOM 1887 CD2 TYR A 550 -25.156 11.298 -0.034 1.00 12.89 C

ANISOU 1887 CD2 TYR A 550 2501 1497 900 372 -409 -131 C

ATOM 1888 CE2 TYR A 550 -26.276 10.894 0.702 1.00 14.13 C ANISOU 1888 CE2 TYR A 550 2627 1640 1100 334 -448 -140 C

ATOM 1889 CZ TYR A 550 -27.220 11.832 1.063 1.00 12.44 C

ANISOU 1889 CZ TYR A 550 2365 1435 929 307 -464 -129 C

ATOM 1890 OH TYR A 550 -28.329 11.472 1.790 1.00 13.29 O ANISOU 1890 OH TYR A 550 2439 1529 1084 270 -498 -136 O

ATOM 1891 C TYR A 550 -22.834 14.015 -3.319 1.00 13.36 C

ANISOU 1891 C TYR A 550 2655 1589 833 487 -302 -85 C

ATOM 1892 O TYR A 550 -21.749 13.422 -3.313 1.00 11.70 O

ANISOU 1892 0 TYR A 550 2462 1378 605 509 -262 -86 O

ATOM 1893 N VAL A 551 -22.996 15.218 -3.859 1.00 15.15 N

ANISOU 1893 N VAL A 551 2880 1826 1052 494 -293 -69 N

ATOM 1894 CA VAL A 551 -21.918 15.907 -4.547 1.00 9.72 C

ANISOU 1894 CA VAL A 551 2214 1147 331 529 -236 -52 C

ATOM 1895 CB VAL A 551 -22.396 16.458 -5.917 1.00 14.94 C

ANISOU 1895 CB VAL A 551 2936 1797 945 553 -258 -48 C

ATOM 1896 CGI VAL A 551 -21.234 17.053 -6.687 1.00 11.94 C

ANISOU 1896 CGI VAL A 551 2589 1423 526 592 -192 -31 C

ATOM 1897 CG2 VAL A 551 -23.064 15.369 -6.727 1.00 15.17 C

ANISOU 1897 CG2 VAL A 551 3033 1796 933 562 -317 -71 C

ATOM 1898 C VAL A 551 -21.437 17.078 -3.705 1.00 12.28 C

ANISOU 1898 C VAL A 551 2469 1500 698 514 -189 -31 C

ATOM 1899 O VAL A 551 -22.207 17.986 -3.417 1.00 8.84 O

ANISOU 1899 0 VAL A 551 1998 1072 288 491 -206 -22 O

ATOM 1900 N SER A 552 -20.162 17.068 -3.328 1.00 11.06 N

ANISOU 1900 N SER A 552 2296 1359 548 526 -131 -23 N

ATOM 1901 CA SER A 552 -19.635 18.105 -2.453 1.00 16.13 C

ANISOU 1901 CA SER A 552 2872 2026 1232 510 -88 -5 C

ATOM 1902 CB SER A 552 -19.936 17.740 -0.999 1.00 11.59 C

ANISOU 1902 CB SER A 552 2238 1458 709 473 -106 -12 C

ATOM 1903 OG SER A 552 -19.426 18.718 -0.126 1.00 12.70 O

ANISOU 1903 OG SER A 552 2319 1620 889 457 -68 4 O

ATOM 1904 C SER A 552 -18.134 18.320 -2.619 1.00 18.89 C

ANISOU 1904 C SER A 552 3219 2386 1574 537 -20 8 C

ATOM 1905 O SER A 552 -17.379 17.368 -2.811 1.00 14.08 O ANISOU 1905 O SER A 552 2636 1769 944 560 -3 -0 O

ATOM 1906 N SER A 553 -17.704 19.574 -2.535 1.00 12.04 N

ANISOU 1906 N SER A 553 2318 1534 724 534 21 28 N

ATOM 1907 CA SER A 553 -16.279 19.887 -2.513 1.00 15.67 C

ANISOU 1907 CA SER A 553 2759 2005 1190 552 88 41 C

ATOM 1908 CB SER A 553 -16.028 21.285 -3.095 1.00 12.41 C

ANISOU 1908 CB SER A 553 2343 1598 773 559 128 63 C

ATOM 1909 OG SER A 553 -16.587 22.291 -2.254 1.00 15.23 O

ANISOU 1909 OG SER A 553 2646 1969 1173 524 118 71 O

ATOM 1910 C SER A 553 -15.766 19.844 -1.080 1.00 14.96 C

ANISOU 1910 C SER A 553 2597 1932 1154 526 99 41 C

ATOM 1911 O SER A 553 -14.591 20.122 -0.824 1.00 10.77 O ANISOU 1911 0 SER A 553 2036 1414 642 534 149 51 O

ATOM 1912 N ASP A 554 -16.649 19.502 -0.143 1.00 7.26 N

ANISOU 1912 N ASP A 554 1596 957 205 494 53 29 N

ATOM 1913 CA ASP A 554 -16.334 19.658 1.282 1.00 8.91 C

ANISOU 1913 CA ASP A 554 1740 1181 464 466 59 30 C

ATOM 1914 CB ASP A 554 -17.319 20.638 1.930 1.00 12.44 C

ANISOU 1914 CB ASP A 554 2151 1633 942 430 37 36 C

ATOM 1915 CG ASP A 554 -17.361 21.981 1.213 1.00 16.25 C

ANISOU 1915 CG ASP A 554 2637 2121 1418 435 62 55 C

ATOM 1916 ODl ASP A 554 -16.282 22.523 0.884 1.00 14.24 O ANISOU 1916 ODl ASP A 554 2375 1875 1161 452 113 67 O

ATOM 1917 OD2 ASP A 554 -18.471 22.496 0.978 1.00 16.47 O

ANISOU 1917 OD2 ASP A 554 2673 2143 1443 423 32 57 O

ATOM 1918 C ASP A 554 -16.296 18.353 2.085 1.00 13.95 C

ANISOU 1918 C ASP A 554 2374 1814 1112 460 35 13 C

ATOM 1919 0 ASP A 554 -16.558 18.361 3.286 1.00 13.02 O

ANISOU 1919 0 ASP A 554 2214 1701 1031 432 20 9 O

ATOM 1920 N PHE A 555 -15.995 17.239 1.422 1.00 10.88 N

ANISOU 1920 N PHE A 555 2034 1412 689 489 32 1 N

ATOM 1921 CA PHE A 555 -15.732 15.990 2.141 1.00 11.13 C

ANISOU 1921 CA PHE A 555 2063 1437 727 489 19 -13 C

ATOM 1922 CB PHE A 555 -15.928 14.778 1.231 1.00 11.59 C

ANISOU 1922 CB PHE A 555 2190 1475 740 515 -1 -29 C

ATOM 1923 CG PHE A 555 -17.346 14.592 0.759 1.00 11.62 C

ANISOU 1923 CG PHE A 555 2228 1460 726 500 -55 -40 C

ATOM 1924 CDl PHE A 555 -18.403 14.651 1.657 1.00 13.57 C

ANISOU 1924 CDl PHE A 555 2442 1704 1008 461 -94 -45 C

ATOM 1925 CD2 PHE A 555 -17.611 14.329 -0.570 1.00 9.75 C

ANISOU 1925 CD2 PHE A 555 2057 1206 440 525 -67 -44 C

ATOM 1926 CE1 PHE A 555 -19.708 14.471 1.234 1.00 12.22 C

ANISOU 1926 CE1 PHE A 555 2295 1515 831 447 -144 -55 C

ATOM 1927 CE2 PHE A 555 -18.920 14.148 -1.010 1.00 10.36 C

ANISOU 1927 CE2 PHE A 555 2163 1265 507 511 -122 -55 C

ATOM 1928 CZ PHE A 555 -19.967 14.220 -0.104 1.00 16.08 C

ANISOU 1928 CZ PHE A 555 2847 1989 1274 471 -161 -60 C

ATOM 1929 C PHE A 555 -14.299 16.026 2.659 1.00 11.19 C

ANISOU 1929 C PHE A 555 2035 1462 756 503 65 -6 C

ATOM 1930 O PHE A 555 -13.355 15.633 1.964 1.00 14.65 O

ANISOU 1930 O PHE A 555 2496 1897 1171 538 99 -3 O

ATOM 1931 N GLY A 556 -14.143 16.509 3.883 1.00 9.90 N

ANISOU 1931 N GLY A 556 1814 1312 636 476 67 -1 N

ATOM 1932 CA GLY A 556 -12.835 16.761 4.457 1.00 8.50 C

ANISOU 1932 CA GLY A 556 1592 1151 486 484 105 7 C

ATOM 1933 C GLY A 556 -13.032 17.721 5.611 1.00 9.10 C

ANISOU 1933 C GLY A 556 1612 1241 606 448 100 14 C

ATOM 1934 O GLY A 556 -14.142 17.833 6.115 1.00 8.28 O ANISOU 1934 0 GLY A 556 1507 1130 510 420 65 9 O

ATOM 1935 N ASN A 557 -11.973 18.417 6.021 1.00 10.00 N

ANISOU 1935 N ASN A 557 1680 1371 748 448 134 25 N

ATOM 1936 CA ASN A 557 -12.072 19.338 7.148 1.00 7.73 C

ANISOU 1936 CA ASN A 557 1342 1093 500 414 129 31 C

ATOM 1937 CB ASN A 557 -10.686 19.636 7.733 1.00 10.19 C

ANISOU 1937 CB ASN A 557 1606 1421 844 418 159 37 C

ATOM 1938 CG ASN A 557 -10.752 20.496 8.986 1.00 15.85 C

ANISOU 1938 CG ASN A 557 2277 2147 1601 383 149 40 C

ATOM 1939 ODl ASN A 557 -11.763 20.513 9.687 1.00 10.05 O

ANISOU 1939 ODl ASN A 557 1546 1405 870 358 117 34 O

ATOM 1940 ND2 ASN A 557 -9.662 21.202 9.280 1.00 13.42 N ANISOU 1940 ND2 ASN A 557 1924 1852 1323 381 177 49 N

ATOM 1941 C ASN A 557 -12.774 20.627 6.727 1.00 12.58 C

ANISOU 1941 C ASN A 557 1955 1710 1116 395 135 42 C

ATOM 1942 0 ASN A 557 -12.142 21.567 6.254 1.00 11.59 O

ANISOU 1942 0 ASN A 557 1814 1594 998 401 172 56 O

ATOM 1943 N HIS A 558 -14.092 20.655 6.902 1.00 9.65 N

ANISOU 1943 N HIS A 558 1599 1329 740 375 99 37 N

ATOM 1944 CA HIS A 558 -14.912 21.785 6.500 1.00 14.35 C

ANISOU 1944 CA HIS A 558 2195 1923 1334 359 99 48 C

ATOM 1945 CB HIS A 558 -15.148 21.739 4.985 1.00 11.23 C

ANISOU 1945 CB HIS A 558 1849 1520 898 386 105 51 C

ATOM 1946 CG HIS A 558 -15.917 22.907 4.449 1.00 11.70 C

ANISOU 1946 CG HIS A 558 1913 1578 953 376 106 63 C

ATOM 1947 CD2 HIS A 558 -15.498 24.059 3.870 1.00 10.18 C

ANISOU 1947 CD2 HIS A 558 1716 1393 760 382 143 80 C

ATOM 1948 ND1 HIS A 558 -17.295 22.969 4.472 1.00 10.79 N

ANISOU 1948 ND1 HIS A 558 1811 1454 836 360 65 60 N

ATOM 1949 CE1 HIS A 558 -17.690 24.110 3.931 1.00 15.02 C

ANISOU 1949 CE1 HIS A 558 2349 1991 1367 357 76 74 C

ATOM 1950 NE2 HIS A 558 -16.620 24.786 3.552 1.00 15.55 N

ANISOU 1950 NE2 HIS A 558 2408 2067 1434 371 123 86 N

ATOM 1951 C HIS A 558 -16.238 21.676 7.242 1.00 10.68 C

ANISOU 1951 C HIS A 558 1728 1449 881 331 57 41 C

ATOM 1952 O HIS A 558 -16.685 20.579 7.534 1.00 7.64 O

ANISOU 1952 0 HIS A 558 1361 1053 490 331 28 27 O

ATOM 1953 N PRO A 559 -16.872 22.814 7.551 1.00 10.15 N

ANISOU 1953 N PRO A 559 1641 1384 833 307 57 51 N

ATOM 1954 CD PRO A 559 -16.390 24.193 7.351 1.00 7.87 C

ANISOU 1954 CD PRO A 559 1330 1106 556 303 92 68 C

ATOM 1955 CA PRO A 559 -18.147 22.763 8.277 1.00 10.89 C

ANISOU 1955 CA PRO A 559 1729 1467 942 281 23 47 C

ATOM 1956 CB PRO A 559 -18.703 24.180 8.102 1.00 9.05 C

ANISOU 1956 CB PRO A 559 1482 1237 719 267 33 62 C

ATOM 1957 CG PRO A 559 -17.479 25.050 7.986 1.00 9.02 C ANISOU 1957 CG PRO A 559 1457 1247 721 273 76 74 C

ATOM 1958 C PRO A 559 -19.139 21.732 7.715 1.00 7.66 C

ANISOU 1958 C PRO A 559 1357 1042 511 287 -15 34 C

ATOM 1959 0 PRO A 559 -19.859 21.100 8.483 1.00 11.00 O

ANISOU 1959 O PRO A 559 1777 1455 949 270 -43 25 O

ATOM 1960 N THR A 560 -19.199 21.579 6.395 1.00 9.78 N

ANISOU 1960 N THR A 560 1663 1307 745 311 -18 34 N

ATOM 1961 CA THR A 560 -20.160 20.648 5.804 1.00 14.17 C

ANISOU 1961 CA THR A 560 2257 1847 1281 316 -58 21 C

ATOM 1962 CB THR A 560 -20.076 20.610 4.266 1.00 16.05 C

ANISOU 1962 CB THR A 560 2542 2080 1475 346 -58 23 C

ATOM 1963 OG1 THR A 560 -20.515 21.862 3.733 1.00 21.07 O

ANISOU 1963 OG1 THR A 560 3174 2721 2110 344 -51 38 O

ATOM 1964 CG2 THR A 560 -20.964 19.499 3.721 1.00 19.94 C

ANISOU 1964 CG2 THR A 560 3076 2554 1946 350 -104 6 C

ATOM 1965 C THR A 560 -19.994 19.222 6.352 1.00 14.58 C

ANISOU 1965 C THR A 560 2318 1888 1331 317 -75 4 C

ATOM 1966 O THR A 560 -20.971 18.585 6.737 1.00 9.96 O

ANISOU 1966 0 THR A 560 1738 1289 759 300 -110 -6 O

ATOM 1967 N SER A 561 -18.764 18.725 6.388 1.00 9.18 N

ANISOU 1967 N SER A 561 1639 1212 639 337 -50 2 N

ATOM 1968 CA SER A 561 -18.520 17.400 6.951 1.00 10.45 C

ANISOU 1968 CA SER A 561 1809 1363 797 341 -63 -14 C

ATOM 1969 CB SER A 561 -17.111 16.904 6.615 1.00 9.55 C

ANISOU 1969 CB SER A 561 1705 1256 665 374 -31 -14 C

ATOM 1970 OG SER A 561 -17.012 16.598 5.227 1.00 10.33 O

ANISOU 1970 OG SER A 561 1851 1348 724 403 -28 -16 O

ATOM 1971 C SER A 561 -18.741 17.379 8.465 1.00 13.33 C

ANISOU 1971 C SER A 561 2137 1727 1199 313 -70 -15 C

ATOM 1972 0 SER A 561 -19.145 16.364 9.005 1.00 10.48 O

ANISOU 1972 0 SER A 561 1787 1352 845 306 -92 -28 O

ATOM 1973 N HIS A 562 -18.466 18.489 9.149 1.00 7.06 N

ANISOU 1973 N HIS A 562 1303 947 432 298 -49 -3 N

ATOM 1974 CA HIS A 562 -18.704 18.537 10.586 1.00 8.68 C

ANISOU 1974 CA HIS A 562 1480 1149 669 272 -55 -4 C

ATOM 1975 CB HIS A 562 -18.196 19.831 11.220 1.00 8.82 C

ANISOU 1975 CB HIS A 562 1459 1182 711 259 -30 10 C

ATOM 1976 CG HIS A 562 -16.773 20.147 10.900 1.00 6.45 C

ANISOU 1976 CG HIS A 562 1145 899 406 279 1 15 C

ATOM 1977 CD2 HIS A 562 -15.746 19.353 10.501 1.00 9.37 C

ANISOU 1977 CD2 HIS A 562 1526 1273 760 307 13 10 C

ATOM 1978 ND1 HIS A 562 -16.271 21.428 10.958 1.00 8.01 N

ANISOU 1978 ND1 HIS A 562 1313 1110 620 271 28 29 N

ATOM 1979 CE1 HIS A 562 -14.994 21.413 10.616 1.00 5.38 C

ANISOU 1979 CE1 HIS A 562 972 790 285 292 54 32 C

ATOM 1980 NE2 HIS A 562 -14.652 20.168 10.329 1.00 11.35 N ANISOU 1980 NE2 HIS A 562 1751 1540 1021 315 46 21 N

ATOM 1981 C HIS A 562 -20.195 18.413 10.875 1.00 9.95 C ANISOU 1981 C HIS A 562 1645 1292 843 247 -85 -8 C

ATOM 1982 O HIS A 562 -20.584 18.146 12.010 1.00 13.15 O

ANISOU 1982 0 HIS A 562 2038 1688 1271 228 -93 -11 O

ATOM 1983 N LEU A 563 -21.028 18.661 9.867 1.00 9.50 N

ANISOU 1983 N LEU A 563 1604 1230 774 248 -101 -6 N

ATOM 1984 CA LEU A 563 -22.472 18.524 10.035 1.00 4.84 C

ANISOU 1984 CA LEU A 563 1015 624 199 226 -132 -9 C

ATOM 1985 CB LEU A 563 -23.231 19.572 9.191 1.00 11.10 C

ANISOU 1985 CB LEU A 563 1806 1421 992 223 -138 3 C

ATOM 1986 CG LEU A 563 -22.986 21.056 9.465 1.00 15.93 C

ANISOU 1986 CG LEU A 563 2386 2047 1618 216 -109 21 C

ATOM 1987 CD 1 LEU A 563 -23.813 21.927 8.522 1.00 13.79 C

ANISOU 1987 CD 1 LEU A 563 2120 1777 1343 217 -120 31 C

ATOM 1988 CD2 LEU A 563 -23.266 21.397 10.932 1.00 7.26 C

ANISOU 1988 CD2 LEU A 563 1255 945 557 189 -101 25 C

ATOM 1989 C LEU A 563 -22.978 17.133 9.659 1.00 12.60 C

ANISOU 1989 C LEU A 563 2032 1588 1167 231 -163 -26 C

ATOM 1990 O LEU A 563 -23.775 16.540 10.396 1.00 9.83 O

ANISOU 1990 O LEU A 563 1677 1219 838 210 -182 -33 O

ATOM 1991 N MET A 564 -22.539 16.625 8.502 1.00 8.59 N

ANISOU 1991 N MET A 564 1560 1079 623 257 -168 -32 N

ATOM 1992 CA MET A 564 -23.193 15.458 7.920 1.00 13.72 C

ANISOU 1992 CA MET A 564 2248 1709 1256 261 -204 -48 C

ATOM 1993 CB MET A 564 -23.905 15.823 6.601 1.00 8.64 C

ANISOU 1993 CB MET A 564 1628 1062 592 268 -229 -48 C

ATOM 1994 CG MET A 564 -23.036 16.502 5.530 1.00 8.70 C

ANISOU 1994 CG MET A 564 1654 1085 567 298 -203 -38 C

ATOM 1995 SD MET A 564 -21.607 15.554 4.998 1.00 12.00 S

ANISOU 1995 SD MET A 564 2110 1502 948 336 -178 -46 S

ATOM 1996 CE MET A 564 -22.395 14.225 4.088 1.00 12.12 C

ANISOU 1996 CE MET A 564 2184 1489 931 343 -226 -67 C

ATOM 1997 C MET A 564 -22.321 14.220 7.712 1.00 11.08 C

ANISOU 1997 C MET A 564 1947 1367 897 285 -199 -62 C

ATOM 1998 O MET A 564 -22.745 13.287 7.039 1.00 8.04 O

ANISOU 1998 0 MET A 564 1600 963 489 291 -227 -76 O

ATOM 1999 N GLN A 565 -21.120 14.181 8.280 1.00 9.63 N

ANISOU 1999 N GLN A 565 1750 1195 715 298 -166 -58 N

ATOM 2000 CA GLN A 565 -20.243 13.047 7.967 1.00 9.19 C

ANISOU 2000 CA GLN A 565 1727 1133 633 326 -160 -69 C

ATOM 2001 CB GLN A 565 -18.838 13.223 8.552 1.00 8.35 C

ANISOU 2001 CB GLN A 565 1597 1045 529 343 -123 -62 C

ATOM 2002 CG GLN A 565 -18.798 13.231 10.075 1.00 7.83 C

ANISOU 2002 CG GLN A 565 1498 980 498 321 -120 -61 C

ATOM 2003 CD GLN A 565 -17.382 13.174 10.624 1.00 15.79 C ANISOU 2003 CD GLN A 565 2489 2005 1504 341 -93 -57 C

ATOM 2004 OEl GLN A 565 -16.440 12.804 9.914 1.00 10.57 O

ANISOU 2004 OEl GLN A 565 1846 1352 819 372 -76 -58 O

ATOM 2005 NE2 GLN A 565 -17.229 13.522 11.896 1.00 12.86 N

ANISOU 2005 NE2 GLN A 565 2085 1639 1161 323 -89 -53 N

ATOM 2006 C GLN A 565 -20.820 11.682 8.372 1.00 10.94 C

ANISOU 2006 C GLN A 565 1974 1329 855 317 -188 -86 C

ATOM 2007 O GLN A 565 -20.422 10.665 7.812 1.00 12.76 O

ANISOU 2007 O GLN A 565 2244 1547 1056 340 -192 -97 O

ATOM 2008 N SER A 566 -21.738 11.641 9.344 1.00 8.62 N

ANISOU 2008 N SER A 566 1660 1025 592 285 -204 -88 N

ATOM 2009 CA SER A 566 -22.281 10.349 9.774 1.00 9.18 C

ANISOU 2009 CA SER A 566 1754 1070 663 275 -227 -103 C

ATOM 2010 CB SER A 566 -22.766 10.386 11.236 1.00 8.91 C

ANISOU 2010 CB SER A 566 1692 1030 665 247 -225 -101 C

ATOM 2011 OG SER A 566 -21.686 10.491 12.147 1.00 8.56 O

ANISOU 2011 OG SER A 566 1629 996 627 258 -196 -94 O

ATOM 2012 C SER A 566 -23.416 9.864 8.868 1.00 14.53 C

ANISOU 2012 C SER A 566 2464 1728 1330 265 -267 -115 C

ATOM 2013 O SER A 566 -23.763 8.687 8.874 1.00 8.83 O

ANISOU 2013 O SER A 566 1772 982 601 262 -287 -131 O

ATOM 2014 N ILE A 567 -23.988 10.766 8.085 1.00 9.74 N

ANISOU 2014 N ILE A 567 1849 1129 723 261 -280 -108 N

ATOM 2015 CA ILE A 567 -25.208 10.439 7.335 1.00 5.33 C

ANISOU 2015 CA ILE A 567 1310 550 164 246 -324 -118 C

ATOM 2016 CB ILE A 567 -25.881 11.716 6.772 1.00 12.37 C

ANISOU 2016 CB ILE A 567 2180 1455 1067 238 -334 -105 C

ATOM 2017 CG2 ILE A 567 -26.921 11.362 5.712 1.00 17.11 C

ANISOU 2017 CG2 ILE A 567 2808 2036 1656 233 -384 -117 C

ATOM 2018 CGI ILE A 567 -26.530 12.490 7.923 1.00 21.53 C

ANISOU 2018 CGI ILE A 567 3284 2619 2276 207 -324 -93 C

ATOM 2019 CD1 ILE A 567 -27.140 13.798 7.519 1.00 25.19 C

ANISOU 2019 CD 1 ILE A 567 3722 3095 2754 200 -329 -78 C

ATOM 2020 C ILE A 567 -25.061 9.340 6.270 1.00 13.11 C

ANISOU 2020 C ILE A 567 2356 1518 1107 268 -347 -136 C

ATOM 2021 O ILE A 567 -25.883 8.423 6.204 1.00 12.08 O

ANISOU 2021 O ILE A 567 2245 1361 983 252 -381 -151 O

ATOM 2022 N PRO A 568 -24.000 9.399 5.456 1.00 11.24 N

ANISOU 2022 N PRO A 568 2149 1294 829 304 -326 -134 N

ATOM 2023 CD PRO A 568 -22.992 10.462 5.272 1.00 9.35 C

ANISOU 2023 CD PRO A 568 1889 1081 582 326 -284 -116 C

ATOM 2024 CA PRO A 568 -23.872 8.339 4.451 1.00 13.47 C

ANISOU 2024 CA PRO A 568 2494 1556 1068 326 -346 -151 C

ATOM 2025 CB PRO A 568 -22.533 8.662 3.782 1.00 14.25 C

ANISOU 2025 CB PRO A 568 2611 1671 1135 367 -304 -141 C

ATOM 2026 CG PRO A 568 -22.450 10.161 3.886 1.00 9.64 C ANISOU 2026 CG PRO A 568 1980 1112 569 362 -283 -121 C

ATOM 2027 C PRO A 568 -23.869 6.927 5.046 1.00 12.01 C

ANISOU 2027 C PRO A 568 2332 1347 885 321 -354 -167 C

ATOM 2028 O PRO A 568 -24.506 6.034 4.489 1.00 15.09 O

ANISOU 2028 O PRO A 568 2762 1710 1260 316 -391 -185 O

ATOM 2029 N GLY A 569 -23.196 6.731 6.172 1.00 12.68 N

ANISOU 2029 N GLY A 569 2391 1439 989 321 -323 -162 N

ATOM 2030 CA GLY A 569 -23.111 5.403 6.756 1.00 10.09 C

ANISOU 2030 CA GLY A 569 2087 1087 659 319 -327 -176 C

ATOM 2031 C GLY A 569 -24.347 4.997 7.534 1.00 12.31 C

ANISOU 2031 C GLY A 569 2351 1345 979 278 -355 -184 C

ATOM 2032 O GLY A 569 -24.468 3.850 7.953 1.00 14.48 O

ANISOU 2032 O GLY A 569 2651 1595 1255 273 -362 -197 O

ATOM 2033 N MET A 570 -25.254 5.944 7.755 1.00 11.47 N

ANISOU 2033 N MET A 570 2204 1246 908 250 -366 -174 N

ATOM 2034 CA MET A 570 -26.520 5.649 8.421 1.00 12.65 C

ANISOU 2034 CA MET A 570 2333 1373 1101 210 -390 -179 C

ATOM 2035 CB MET A 570 -26.922 6.786 9.352 1.00 10.75 C

ANISOU 2035 CB MET A 570 2033 1148 905 187 -373 -161 C

ATOM 2036 CG MET A 570 -26.060 6.809 10.608 1.00 12.46 C

ANISOU 2036 CG MET A 570 2232 1375 1129 193 -332 -153 C

ATOM 2037 SD MET A 570 -26.436 8.219 11.625 1.00 17.17 S

ANISOU 2037 SD MET A 570 2766 1988 1769 170 -310 -132 S

ATOM 2038 CE MET A 570 -25.579 7.755 13.141 1.00 18.95 C

ANISOU 2038 CE MET A 570 2989 2211 1999 175 -275 -129 C

ATOM 2039 C MET A 570 -27.651 5.337 7.454 1.00 15.76 C

ANISOU 2039 C MET A 570 2747 1745 1496 194 -440 -192 C

ATOM 2040 O MET A 570 -28.744 4.968 7.877 1.00 11.75 O

ANISOU 2040 O MET A 570 2225 1215 1026 161 -464 -198 O

ATOM 2041 N HIS A 571 -27.394 5.478 6.160 1.00 7.23 N

ANISOU 2041 N HIS A 571 1702 670 374 218 -457 -197 N

ATOM 2042 CA HIS A 571 -28.414 5.118 5.182 1.00 12.96 C

ANISOU 2042 CA HIS A 571 2454 1374 1095 206 -511 -211 C

ATOM 2043 CB HIS A 571 -27.988 5.532 3.777 1.00 14.28 C

ANISOU 2043 CB HIS A 571 2662 1552 1212 238 -522 -212 C

ATOM 2044 CG HIS A 571 -28.369 6.939 3.428 1.00 14.87 C

ANISOU 2044 CG HIS A 571 2701 1650 1299 235 -526 -195 C

ATOM 2045 CD2 HIS A 571 -27.618 8.047 3.211 1.00 15.74 C

ANISOU 2045 CD2 HIS A 571 2798 1790 1393 258 -491 -177 C

ATOM 2046 ND1 HIS A 571 -29.678 7.322 3.242 1.00 14.50 N

ANISOU 2046 ND1 HIS A 571 2629 1594 1285 207 -570 -196 N

ATOM 2047 CE1 HIS A 571 -29.722 8.606 2.932 1.00 13.70 C

ANISOU 2047 CE1 HIS A 571 2502 1516 1186 214 -562 -179 C

ATOM 2048 NE2 HIS A 571 -28.484 9.070 2.909 1.00 14.16 N

ANISOU 2048 NE2 HIS A 571 2568 1599 1215 244 -514 -167 N

ATOM 2049 C HIS A 571 -28.725 3.622 5.249 1.00 19.36 C ANISOU 2049 C HIS A 571 3306 2148 1903 195 -534 -233 C

ATOM 2050 O HIS A 571 -27.833 2.804 5.466 1.00 15.10 O

ANISOU 2050 O HIS A 571 2799 1603 1337 216 -510 -240 O

ATOM 2051 N ASN A 572 -29.999 3.275 5.081 1.00 13.68 N

ANISOU 2051 N ASN A 572 2582 1404 1214 162 -581 -245 N

ATOM 2052 CA ASN A 572 -30.432 1.880 5.078 1.00 10.22 C

ANISOU 2052 CA ASN A 572 2181 926 777 147 -608 -267 C

ATOM 2053 CB ASN A 572 -31.944 1.808 5.293 1.00 14.14 C

ANISOU 2053 CB ASN A 572 2642 1400 1332 100 -650 -272 C

ATOM 2054 CG ASN A 572 -32.497 0.404 5.127 1.00 17.66 C

ANISOU 2054 CG ASN A 572 3128 1802 1781 81 -685 -297 C

ATOM 2055 ODl ASN A 572 -31.752 -0.588 5.117 1.00 15.23 O ANISOU 2055 ODl ASN A 572 2871 1479 1436 100 -670 -309 O

ATOM 2056 ND2 ASN A 572 -33.814 0.313 4.981 1.00 12.70 N

ANISOU 2056 ND2 ASN A 572 2475 1152 1198 43 -732 -305 N

ATOM 2057 C ASN A 572 -30.085 1.204 3.757 1.00 16.09 C

ANISOU 2057 C ASN A 572 2997 1655 1461 174 -637 -285 C

ATOM 2058 O ASN A 572 -30.684 1.509 2.728 1.00 15.55 O

ANISOU 2058 O ASN A 572 2945 1583 1381 172 -682 -291 O

ATOM 2059 N PRO A 573 -29.127 0.273 3.786 1.00 18.28 N

ANISOU 2059 N PRO A 573 3324 1923 1700 200 -613 -294 N

ATOM 2060 CD PRO A 573 -28.465 -0.247 4.997 1.00 11.15 C

ANISOU 2060 CD PRO A 573 2408 1019 808 202 -567 -289 C

ATOM 2061 CA PRO A 573 -28.619 -0.358 2.562 1.00 16.84 C

ANISOU 2061 CA PRO A 573 3217 1727 1454 232 -630 -309 C

ATOM 2062 CB PRO A 573 -27.457 -1.218 3.069 1.00 20.42 C

ANISOU 2062 CB PRO A 573 3701 2176 1881 260 -584 -311 C

ATOM 2063 CG PRO A 573 -27.777 -1.488 4.498 1.00 22.85 C

ANISOU 2063 CG PRO A 573 3962 2478 2241 230 -566 -306 C

ATOM 2064 C PRO A 573 -29.635 -1.242 1.834 1.00 15.85 C

ANISOU 2064 C PRO A 573 3134 1561 1326 210 -693 -334 C

ATOM 2065 O PRO A 573 -29.443 -1.529 0.656 1.00 15.76 O

ANISOU 2065 O PRO A 573 3187 1539 1264 234 -719 -347 O

ATOM 2066 N ASP A 574 -30.688 -1.673 2.519 1.00 16.05 N

ANISOU 2066 N ASP A 574 3129 1564 1407 165 -718 -341 N

ATOM 2067 CA ASP A 574 -31.746 -2.454 1.874 1.00 18.62 C

ANISOU 2067 CA ASP A 574 3484 1849 1739 138 -782 -365 C

ATOM 2068 CB ASP A 574 -32.670 -3.074 2.937 1.00 20.79 C

ANISOU 2068 CB ASP A 574 3720 2097 2081 89 -789 -371 C

ATOM 2069 CG ASP A 574 -33.744 -3.959 2.329 1.00 31.88 C

ANISOU 2069 CG ASP A 574 5154 3459 3500 57 -855 -397 C

ATOM 2070 ODl ASP A 574 -33.405 -4.747 1.428 1.00 21.12 O

ANISOU 2070 ODl ASP A 574 3867 2075 2084 77 -879 -416 O

ATOM 2071 OD2 ASP A 574 -34.919 -3.868 2.745 1.00 19.44 O

ANISOU 2071 OD2 ASP A 574 3527 1870 1990 12 -883 -397 O

ATOM 2072 C ASP A 574 -32.566 -1.618 0.881 1.00 17.49 C ANISOU 2072 C ASP A 574 3333 1714 1600 130 -837 -366 C

ATOM 2073 O ASP A 574 -33.165 -2.155 -0.058 1.00 14.96 O

ANISOU 2073 O ASP A 574 3056 1365 1261 123 -896 -387 O

ATOM 2074 N LYS A 575 -32.593 -0.304 1.080 1.00 14.07 N

ANISOU 2074 N LYS A 575 2843 1317 1187 133 -819 -343 N

ATOM 2075 CA LYS A 575 -33.449 0.562 0.266 1.00 20.65 C

ANISOU 2075 CA LYS A 575 3659 2158 2030 124 -869 -341 C

ATOM 2076 CB LYS A 575 -34.572 1.160 1.120 1.00 16.96 C

ANISOU 2076 CB LYS A 575 3106 1694 1643 81 -879 -330 C

ATOM 2077 CG LYS A 575 -35.531 0.136 1.717 1.00 18.93 C

ANISOU 2077 CG LYS A 575 3340 1906 1948 36 -905 -345 C

ATOM 2078 CD LYS A 575 -36.414 -0.503 0.657 1.00 20.94 C

ANISOU 2078 CD LYS A 575 3633 2127 2197 20 -985 -371 C

ATOM 2079 CE LYS A 575 -37.429 -1.444 1.294 1.00 26.77 C

ANISOU 2079 CE LYS A 575 4346 2827 3000 -30 -1010 -385 C

ATOM 2080 NZ LYS A 575 -38.278 -2.121 0.279 1.00 28.55 N

ANISOU 2080 NZ LYS A 575 4609 3017 3223 -49 -1092 -412 N

ATOM 2081 C LYS A 575 -32.703 1.699 -0.430 1.00 22.13 C

ANISOU 2081 C LYS A 575 3856 2380 2172 165 -848 -324 C

ATOM 2082 O LYS A 575 -33.272 2.396 -1.279 1.00 21.61 O

ANISOU 2082 O LYS A 575 3792 2320 2101 167 -889 -323 O

ATOM 2083 N PHE A 576 -31.443 1.903 -0.062 1.00 12.89 N

ANISOU 2083 N PHE A 576 2691 1233 973 197 -783 -311 N

ATOM 2084 CA PHE A 576 -30.662 3.006 -0.625 1.00 11.32 C

ANISOU 2084 CA PHE A 576 2497 1067 737 233 -753 -293 C

ATOM 2085 CB PHE A 576 -30.618 4.193 0.352 1.00 13.65 C

ANISOU 2085 CB PHE A 576 2712 1396 1078 222 -712 -267 C

ATOM 2086 CG PHE A 576 -31.964 4.762 0.641 1.00 15.91 C

ANISOU 2086 CG PHE A 576 2940 1680 1424 183 -750 -262 C

ATOM 2087 CDl PHE A 576 -32.454 5.827 -0.105 1.00 16.29 C ANISOU 2087 CDl PHE A 576 2976 1742 1470 188 -777 -253 C

ATOM 2088 CD2 PHE A 576 -32.768 4.200 1.618 1.00 16.95 C ANISOU 2088 CD2 PHE A 576 3032 1793 1615 142 -760 -268 C

ATOM 2089 CEl PHE A 576 -33.720 6.346 0.139 1.00 15.90 C ANISOU 2089 CEl PHE A 576 2872 1690 1478 154 -814 -248 C

ATOM 2090 CE2 PHE A 576 -34.034 4.706 1.866 1.00 14.66 C ANISOU 2090 CE2 PHE A 576 2687 1499 1385 107 -793 -263 C

ATOM 2091 CZ PHE A 576 -34.511 5.788 1.122 1.00 14.56 C

ANISOU 2091 CZ PHE A 576 2659 1503 1371 114 -821 -253 C

ATOM 2092 C PHE A 576 -29.259 2.550 -0.959 1.00 17.29 C

ANISOU 2092 C PHE A 576 3310 1827 1433 278 -708 -294 C

ATOM 2093 O PHE A 576 -28.690 1.693 -0.283 1.00 16.11 O

ANISOU 2093 O PHE A 576 3168 1668 1283 280 -678 -299 O

ATOM 2094 N GLU A 577 -28.718 3.111 -2.029 1.00 14.88 N

ANISOU 2094 N GLU A 577 3045 1533 1075 315 -703 -288 N

ATOM 2095 CA GLU A 577 -27.340 2.864 -2.405 1.00 18.32 C ANISOU 2095 CA GLU A 577 3529 1976 1456 361 -652 -285 C

ATOM 2096 CB GLU A 577 -27.258 2.125 -3.739 1.00 19.90 C

ANISOU 2096 CB GLU A 577 3824 2147 1591 388 -684 -304 C

ATOM 2097 CG GLU A 577 -25.869 1.593 -4.044 1.00 22.79 C

ANISOU 2097 CG GLU A 577 4243 2512 1903 435 -630 -303 C

ATOM 2098 CD GLU A 577 -25.793 0.813 -5.349 1.00 27.20 C

ANISOU 2098 CD GLU A 577 4903 3038 2393 464 -659 -323 C

ATOM 2099 OEl GLU A 577 -26.783 0.780 -6.113 1.00 19.66 O

ANISOU 2099 OEl GLU A 577 3979 2062 1427 450 -725 -337 O

ATOM 2100 OE2 GLU A 577 -24.727 0.228 -5.611 1.00 20.25 O

ANISOU 2100 OE2 GLU A 577 4071 2151 1472 503 -616 -323 O

ATOM 2101 C GLU A 577 -26.707 4.242 -2.516 1.00 17.79 C

ANISOU 2101 C GLU A 577 3430 1946 1384 383 -609 -259 C

ATOM 2102 O GLU A 577 -27.133 5.059 -3.340 1.00 15.55 O

ANISOU 2102 O GLU A 577 3155 1668 1085 389 -633 -254 O

ATOM 2103 N VAL A 578 -25.708 4.499 -1.678 1.00 13.68 N

ANISOU 2103 N VAL A 578 2872 1450 877 394 -547 -243 N

ATOM 2104 CA VAL A 578 -25.168 5.854 -1.519 1.00 12.16 C

ANISOU 2104 CA VAL A 578 2634 1293 694 405 -505 -218 C

ATOM 2105 CB VAL A 578 -24.910 6.198 -0.028 1.00 18.89 C

ANISOU 2105 CB VAL A 578 3410 2167 1601 383 -468 -204 C

ATOM 2106 CGI VAL A 578 -24.362 7.623 0.109 1.00 16.59 C

ANISOU 2106 CGI VAL A 578 3073 1909 1322 392 -425 -179 C

ATOM 2107 CG2 VAL A 578 -26.184 6.051 0.780 1.00 20.15 C

ANISOU 2107 CG2 VAL A 578 3527 2314 1815 335 -507 -211 C

ATOM 2108 C VAL A 578 -23.867 6.037 -2.284 1.00 15.96 C

ANISOU 2108 C VAL A 578 3155 1782 1127 454 -455 -208 C

ATOM 2109 O VAL A 578 -22.910 5.288 -2.083 1.00 13.75 O

ANISOU 2109 O VAL A 578 2894 1498 833 477 -419 -210 O

ATOM 2110 N PHE A 579 -23.843 7.058 -3.137 1.00 14.93 N

ANISOU 2110 N PHE A 579 3034 1663 975 471 -451 -196 N

ATOM 2111 CA PHE A 579 -22.662 7.444 -3.885 1.00 11.37 C

ANISOU 2111 CA PHE A 579 2616 1222 483 516 -398 -183 C

ATOM 2112 CB PHE A 579 -22.979 7.523 -5.378 1.00 12.09 C

ANISOU 2112 CB PHE A 579 2783 1294 515 542 -428 -189 C

ATOM 2113 CG PHE A 579 -23.394 6.210 -5.998 1.00 17.34 C

ANISOU 2113 CG PHE A 579 3523 1922 1142 547 -475 -216 C

ATOM 2114 CD1 PHE A 579 -22.566 5.566 -6.912 1.00 13.65 C

ANISOU 2114 CD1 PHE A 579 3136 1436 615 591 -451 -222 C

ATOM 2115 CD2 PHE A 579 -24.622 5.646 -5.702 1.00 16.31 C

ANISOU 2115 CD2 PHE A 579 3386 1775 1037 508 -542 -235 C

ATOM 2116 CE1 PHE A 579 -22.944 4.370 -7.502 1.00 19.65 C

ANISOU 2116 CE1 PHE A 579 3970 2160 1338 596 -494 -247 C

ATOM 2117 CE2 PHE A 579 -25.016 4.444 -6.287 1.00 18.43 C

ANISOU 2117 CE2 PHE A 579 3725 2006 1271 510 -587 -261 C

ATOM 2118 CZ PHE A 579 -24.172 3.808 -7.193 1.00 18.89 C ANISOU 2118 CZ PHE A 579 3865 2045 1266 555 -564 -267 C

ATOM 2119 C PHE A 579 -22.224 8.827 -3.422 1.00 17.18 C

ANISOU 2119 C PHE A 579 3287 1991 1248 514 -354 -157 C

ATOM 2120 O PHE A 579 -23.015 9.760 -3.445 1.00 16.70 O

ANISOU 2120 O PHE A 579 3197 1940 1207 494 -377 -150 O

ATOM 2121 N CYS A 580 -20.971 8.963 -3.002 1.00 13.03 N

ANISOU 2121 N CYS A 580 2739 1484 727 534 -292 -145 N

ATOM 2122 CA CYS A 580 -20.440 10.277 -2.657 1.00 9.17 C

ANISOU 2122 CA CYS A 580 2195 1026 262 534 -248 -121 C

ATOM 2123 CB CYS A 580 -19.762 10.259 -1.283 1.00 7.86 C

ANISOU 2123 CB CYS A 580 1965 880 143 520 -213 -114 C

ATOM 2124 SG CYS A 580 -20.949 10.149 0.084 1.00 17.72 S

ANISOU 2124 SG CYS A 580 3155 2128 1452 466 -256 -121 S

ATOM 2125 C CYS A 580 -19.474 10.708 -3.746 1.00 17.48 C

ANISOU 2125 C CYS A 580 3291 2082 1267 578 -203 -109 C

ATOM 2126 O CYS A 580 -18.501 10.006 -4.029 1.00 15.07 O

ANISOU 2126 O CYS A 580 3021 1772 934 610 -169 -112 O

ATOM 2127 N TYR A 581 -19.775 11.846 -4.370 1.00 14.18 N

ANISOU 2127 N TYR A 581 2875 1673 840 581 -201 -96 N

ATOM 2128 CA TYR A 581 -18.941 12.419 -5.419 1.00 11.71 C

ANISOU 2128 CA TYR A 581 2604 1363 483 621 -155 -82 C

ATOM 2129 CB TYR A 581 -19.794 12.848 -6.617 1.00 13.50 C

ANISOU 2129 CB TYR A 581 2887 1573 669 631 -193 -84 C

ATOM 2130 CG TYR A 581 -20.515 11.694 -7.271 1.00 17.37 C

ANISOU 2130 CG TYR A 581 3447 2031 1122 636 -252 -109 C

ATOM 2131 CD1 TYR A 581 -19.887 10.917 -8.244 1.00 17.55 C ANISOU 2131 CD1 TYR A 581 3552 2030 1084 678 -235 -116 C

ATOM 2132 CEl TYR A 581 -20.548 9.849 -8.852 1.00 14.02 C

ANISOU 2132 CEl TYR A 581 3174 1552 602 681 -292 -141 C

ATOM 2133 CD2 TYR A 581 -21.818 11.372 -6.913 1.00 18.35 C ANISOU 2133 CD2 TYR A 581 3556 2145 1273 599 -323 -124 C

ATOM 2134 CE2 TYR A 581 -22.482 10.303 -7.511 1.00 16.42 C

ANISOU 2134 CE2 TYR A 581 3374 1868 995 601 -380 -148 C

ATOM 2135 CZ TYR A 581 -21.841 9.550 -8.476 1.00 13.53 C

ANISOU 2135 CZ TYR A 581 3094 1481 568 642 -365 -157 C

ATOM 2136 OH TYR A 581 -22.504 8.490 -9.054 1.00 18.56 O

ANISOU 2136 OH TYR A 581 3796 2084 1172 642 -424 -182 O

ATOM 2137 C TYR A 581 -18.151 13.601 -4.877 1.00 13.57 C

ANISOU 2137 C TYR A 581 2776 1629 750 618 -97 -58 C

ATOM 2138 O TYR A 581 -18.694 14.686 -4.690 1.00 13.28 O

ANISOU 2138 O TYR A 581 2702 1605 737 597 -105 -47 O

ATOM 2139 N ALA A 582 -16.865 13.377 -4.617 1.00 11.45 N

ANISOU 2139 N ALA A 582 2493 1371 486 639 -40 -51 N

ATOM 2140 CA ALA A 582 -16.006 14.413 -4.064 1.00 13.85 C

ANISOU 2140 CA ALA A 582 2734 1702 828 635 15 -30 C

ATOM 2141 CB ALA A 582 -14.839 13.779 -3.310 1.00 13.89 C ANISOU 2141 CB ALA A 582 2706 1716 856 645 55 -30 C

ATOM 2142 C ALA A 582 -15.503 15.355 -5.159 1.00 13.61 C

ANISOU 2142 C ALA A 582 2734 1671 767 665 61 -11 C

ATOM 2143 O ALA A 582 -15.014 14.911 -6.197 1.00 16.57 O

ANISOU 2143 O ALA A 582 3174 2029 1092 704 84 -12 O

ATOM 2144 N LEU A 583 -15.637 16.659 -4.928 1.00 12.99 N

ANISOU 2144 N LEU A 583 2611 1609 715 647 75 5 N

ATOM 2145 CA LEU A 583 -15.133 17.648 -5.871 1.00 10.57 C

ANISOU 2145 CA LEU A 583 2328 1303 384 672 123 25 C

ATOM 2146 CB LEU A 583 -16.110 18.827 -6.001 1.00 11.35 C

ANISOU 2146 CB LEU A 583 2416 1406 490 651 97 34 C

ATOM 2147 CG LEU A 583 -17.551 18.483 -6.390 1.00 15.56 C

ANISOU 2147 CG LEU A 583 2990 1923 999 640 21 18 C

ATOM 2148 CDl LEU A 583 -18.402 19.752 -6.584 1.00 14.04 C

ANISOU 2148 CDl LEU A 583 2785 1736 814 625 3 31 C

ATOM 2149 CD2 LEU A 583 -17.572 17.620 -7.661 1.00 13.40 C

ANISOU 2149 CD2 LEU A 583 2811 1622 658 679 7 7 C

ATOM 2150 C LEU A 583 -13.749 18.151 -5.453 1.00 18.88 C

ANISOU 2150 C LEU A 583 3329 2374 1470 680 197 43 C

ATOM 2151 O LEU A 583 -13.135 18.960 -6.149 1.00 22.31 O

ANISOU 2151 O LEU A 583 3777 2809 1892 701 249 61 O

ATOM 2152 N SER A 584 -13.264 17.668 -4.315 1.00 11.82 N

ANISOU 2152 N SER A 584 2378 1494 619 663 199 37 N

ATOM 2153 CA SER A 584 -11.964 18.076 -3.803 1.00 9.63 C

ANISOU 2153 CA SER A 584 2045 1234 380 668 260 52 C

ATOM 2154 CB SER A 584 -12.107 18.781 -2.443 1.00 15.41 C

ANISOU 2154 CB SER A 584 2694 1989 1173 624 248 55 C

ATOM 2155 OG SER A 584 -12.577 17.876 -1.452 1.00 19.91 O

ANISOU 2155 OG SER A 584 3245 2559 1761 602 200 38 O

ATOM 2156 C SER A 584 -11.089 16.853 -3.648 1.00 13.43 C

ANISOU 2156 C SER A 584 2534 1712 859 692 277 43 C

ATOM 2157 O SER A 584 -11.600 15.752 -3.444 1.00 17.00 O

ANISOU 2157 O SER A 584 3012 2152 1295 691 234 24 O

ATOM 2158 N PRO A 585 -9.764 17.043 -3.760 1.00 15.47 N

ANISOU 2158 N PRO A 585 2768 1977 1132 716 343 57 N

ATOM 2159 CD PRO A 585 -9.114 18.307 -4.143 1.00 20.36 C

ANISOU 2159 CD PRO A 585 3364 2606 1768 720 401 80 C

ATOM 2160 CA PRO A 585 -8.797 15.989 -3.448 1.00 19.54 C

ANISOU 2160 CA PRO A 585 3275 2492 1656 739 364 52 C

ATOM 2161 CB PRO A 585 -7.446 16.622 -3.815 1.00 23.46 C

ANISOU 2161 CB PRO A 585 3743 2997 2172 763 443 74 C

ATOM 2162 CG PRO A 585 -7.675 18.080 -3.760 1.00 34.55 C

ANISOU 2162 CG PRO A 585 5114 4414 3600 737 455 89 C

ATOM 2163 C PRO A 585 -8.848 15.643 -1.963 1.00 17.48 C

ANISOU 2163 C PRO A 585 2950 2248 1445 706 330 42 C

ATOM 2164 O PRO A 585 -9.350 16.433 -1.155 1.00 12.32 O ANISOU 2164 O PRO A 585 2246 1608 825 667 306 44 O

ATOM 2165 N ASP A 586 -8.355 14.455 -1.627 1.00 14.02 N

ANISOU 2165 N ASP A 586 2516 1805 1006 724 327 32 N

ATOM 2166 CA ASP A 586 -8.333 13.953 -0.258 1.00 19.78 C

ANISOU 2166 CA ASP A 586 3195 2546 1775 700 295 21 C

ATOM 2167 CB ASP A 586 -7.884 12.483 -0.299 1.00 15.85 C

ANISOU 2167 CB ASP A 586 2731 2034 1256 732 294 9 C

ATOM 2168 CG ASP A 586 -7.771 11.841 1.080 1.00 17.14 C

ANISOU 2168 CG ASP A 586 2851 2207 1456 714 264 -1 C

ATOM 2169 ODl ASP A 586 -7.770 12.551 2.099 1.00 17.20 O

ANISOU 2169 ODl ASP A 586 2795 2233 1508 682 254 3 O

ATOM 2170 OD2 ASP A 586 -7.669 10.600 1.134 1.00 20.58 O ANISOU 2170 OD2 ASP A 586 3318 2628 1872 734 252 -14 O

ATOM 2171 C ASP A 586 -7.378 14.802 0.577 1.00 19.68 C

ANISOU 2171 C ASP A 586 3100 2558 1819 687 328 36 C

ATOM 2172 0 ASP A 586 -6.198 14.901 0.249 1.00 15.11 O

ANISOU 2172 O ASP A 586 2504 1985 1254 714 381 49 O

ATOM 2173 N ASP A 587 -7.879 15.425 1.644 1.00 16.69 N

ANISOU 2173 N ASP A 587 2671 2193 1477 645 296 35 N

ATOM 2174 CA ASP A 587 -7.039 16.311 2.460 1.00 18.42 C

ANISOU 2174 CA ASP A 587 2815 2434 1751 628 321 47 C

ATOM 2175 CB ASP A 587 -7.814 17.551 2.960 1.00 17.20 C

ANISOU 2175 CB ASP A 587 2629 2288 1619 585 301 52 C

ATOM 2176 CG ASP A 587 -8.929 17.208 3.952 1.00 17.19 C

ANISOU 2176 CG ASP A 587 2625 2283 1622 552 241 37 C

ATOM 2177 OD1 ASP A 587 -9.117 16.014 4.277 1.00 12.65 O ANISOU 2177 ODl ASP A 587 2073 1700 1035 560 213 22 O

ATOM 2178 OD2 ASP A 587 -9.622 18.153 4.406 1.00 11.79 O

ANISOU 2178 OD2 ASP A 587 1920 1606 956 518 224 41 O

ATOM 2179 C ASP A 587 -6.335 15.608 3.617 1.00 19.27 C

ANISOU 2179 C ASP A 587 2878 2550 1893 628 309 40 C

ATOM 2180 O ASP A 587 -5.707 16.258 4.447 1.00 14.28 O

ANISOU 2180 O ASP A 587 2183 1936 1308 611 318 47 O

ATOM 2181 N GLY A 588 -6.443 14.282 3.660 1.00 17.30 N

ANISOU 2181 N GLY A 588 2665 2288 1619 648 288 26 N

ATOM 2182 CA GLY A 588 -5.781 13.491 4.680 1.00 20.35 C ANISOU 2182 CA GLY A 588 3020 2681 2032 654 277 19 C

ATOM 2183 C GLY A 588 -6.461 13.456 6.045 1.00 17.67 C

ANISOU 2183 C GLY A 588 2655 2345 1715 616 226 9 C

ATOM 2184 O GLY A 588 -5.924 12.845 6.959 1.00 20.72 O

ANISOU 2184 O GLY A 588 3017 2736 2122 621 214 3 O

ATOM 2185 N THR A 589 -7.629 14.088 6.191 1.00 14.25 N

ANISOU 2185 N THR A 589 2229 1909 1277 581 197 6 N

ATOM 2186 CA THR A 589 -8.277 14.163 7.505 1.00 12.88 C

ANISOU 2186 CA THR A 589 2031 1737 1127 544 155 -2 C

ATOM 2187 CB THR A 589 -9.051 15.486 7.703 1.00 10.22 C ANISOU 2187 CB THR A 589 1672 1407 806 506 147 5 C

ATOM 2188 OG1 THR A 589 -10.108 15.569 6.737 1.00 11.13 O ANISOU 2188 OG1 THR A 589 1835 1509 887 504 137 4 O ATOM 2189 CG2 THR A 589 -8.110 16.671 7.556 1.00 14.55 C ANISOU 2189 CG2 THR A 589 2173 1973 1383 506 188 22 C

ATOM 2190 C THR A 589 -9.234 13.002 7.746 1.00 11.68 C

ANISOU 2190 C THR A 589 1925 1565 949 541 114 -19 C

ATOM 2191 O THR A 589 -9.680 12.354 6.796 1.00 12.46 O

ANISOU 2191 O THR A 589 2077 1647 1009 558 111 -26 O

ATOM 2192 N ASN A 590 -9.559 12.753 9.015 1.00 10.40 N

ANISOU 2192 N ASN A 590 1743 1401 807 518 83 -27 N

ATOM 2193 CA ASN A 590 -10.495 11.682 9.358 1.00 10.98 C

ANISOU 2193 CA ASN A 590 1857 1453 861 511 46 -42 C

ATOM 2194 CB ASN A 590 -10.556 11.468 10.874 1.00 9.57 C

ANISOU 2194 CB ASN A 590 1652 1274 709 491 22 -47 C

ATOM 2195 CG ASN A 590 -9.286 10.837 11.417 1.00 18.74 C

ANISOU 2195 CG ASN A 590 2795 2442 1882 519 33 -48 C ATOM 2196 OD1 ASN A 590 -8.434 10.405 10.648 1.00 18.11 O ANISOU 2196 OD1 ASN A 590 2724 2365 1789 554 59 -45 O ATOM 2197 ND2 ASN A 590 -9.158 10.775 12.739 1.00 11.02 N ANISOU 2197 ND2 ASN A 590 1793 1466 927 505 14 -50 N

ATOM 2198 C ASN A 590 -11.895 11.904 8.796 1.00 12.45 C

ANISOU 2198 C ASN A 590 2076 1627 1029 488 24 -47 C

ATOM 2199 O ASN A 590 -12.664 10.954 8.648 1.00 9.87 O

ANISOU 2199 O ASN A 590 1791 1278 680 487 -2 -60 O

ATOM 2200 N PHE A 591 -12.240 13.154 8.508 1.00 10.23 N

ANISOU 2200 N PHE A 591 1773 1356 758 469 32 -36 N

ATOM 2201 CA PHE A 591 -13.561 13.441 7.946 1.00 9.08 C

ANISOU 2201 CA PHE A 591 1654 1198 597 449 9 -38 C

ATOM 2202 CB PHE A 591 -13.806 14.962 7.845 1.00 10.95 C

ANISOU 2202 CB PHE A 591 1859 1450 853 429 21 -24 C

ATOM 2203 CG PHE A 591 -13.619 15.695 9.148 1.00 8.86 C

ANISOU 2203 CG PHE A 591 1541 1196 628 402 22 -18 C

ATOM 2204 CD1 PHE A 591 -14.521 15.534 10.185 1.00 8.45 C

ANISOU 2204 CD 1 PHE A 591 1484 1135 593 373 -8 -24 C

ATOM 2205 CD2 PHE A 591 -12.523 16.539 9.338 1.00 10.89 C

ANISOU 2205 CD2 PHE A 591 1757 1473 907 406 55 -5 C

ATOM 2206 CE1 PHE A 591 -14.346 16.202 11.394 1.00 12.69 C

ANISOU 2206 CE1 PHE A 591 1980 1681 1163 350 -6 -19 C

ATOM 2207 CE2 PHE A 591 -12.334 17.203 10.541 1.00 12.29 C

ANISOU 2207 CE2 PHE A 591 1891 1659 1119 382 52 -2 C

ATOM 2208 CZ PHE A 591 -13.245 17.037 11.575 1.00 9.88 C

ANISOU 2208 CZ PHE A 591 1586 1344 826 355 21 -9 C

ATOM 2209 C PHE A 591 -13.669 12.793 6.569 1.00 13.12 C

ANISOU 2209 C PHE A 591 2223 1697 1066 478 10 -44 C

ATOM 2210 O PHE A 591 -14.683 12.188 6.204 1.00 10.59 O ANISOU 2210 O PHE A 591 1942 1357 726 471 -22 -56 O

ATOM 2211 N ARG A 592 -12.598 12.900 5.802 1.00 11.75 N

ANISOU 2211 N ARG A 592 2054 1531 879 510 49 -36 N

ATOM 2212 CA ARG A 592 -12.590 12.318 4.477 1.00 10.78 C

ANISOU 2212 CA ARG A 592 1990 1394 711 541 56 -40 C

ATOM 2213 CB ARG A 592 -11.460 12.939 3.649 1.00 8.52 C

ANISOU 2213 CB ARG A 592 1699 1120 419 572 108 -24 C

ATOM 2214 CG ARG A 592 -11.198 12.286 2.297 1.00 16.27 C

ANISOU 2214 CG ARG A 592 2745 2085 1352 612 126 -27 C

ATOM 2215 CD ARG A 592 -12.295 12.580 1.301 1.00 9.29 C

ANISOU 2215 CD ARG A 592 1911 1187 433 606 102 -30 C

ATOM 2216 NE ARG A 592 -11.824 12.388 -0.075 1.00 11.42 N

ANISOU 2216 NE ARG A 592 2237 1444 656 647 133 -27 N

ATOM 2217 CZ ARG A 592 -11.851 13.335 -1.012 1.00 12.55 C

ANISOU 2217 CZ ARG A 592 2397 1589 782 656 156 -14 C

ATOM 2218 NHl ARG A 592 -12.320 14.552 -0.733 1.00 11.63 N ANISOU 2218 NHl ARG A 592 2242 1486 690 627 151 -3 N

ATOM 2219 NH2 ARG A 592 -11.403 13.075 -2.233 1.00 10.91 N ANISOU 2219 NH2 ARG A 592 2248 1367 529 696 186 -11 N

ATOM 2220 C ARG A 592 -12.504 10.788 4.585 1.00 9.46 C

ANISOU 2220 C ARG A 592 1862 1208 524 560 39 -56 C

ATOM 2221 O ARG A 592 -13.223 10.072 3.887 1.00 11.18 O

ANISOU 2221 O ARG A 592 2136 1405 708 565 15 -69 O

ATOM 2222 N VAL A 593 -11.675 10.293 5.498 1.00 9.36 N

ANISOU 2222 N VAL A 593 1821 1202 533 568 50 -57 N

ATOM 2223 CA VAL A 593 -11.584 8.843 5.736 1.00 9.49 C

ANISOU 2223 CA VAL A 593 1872 1200 533 585 35 -72 C

ATOM 2224 CB VAL A 593 -10.667 8.523 6.931 1.00 12.45 C

ANISOU 2224 CB VAL A 593 2205 1587 939 590 44 -70 C

ATOM 2225 CGI VAL A 593 -10.757 7.030 7.289 1.00 13.89 C ANISOU 2225 CGI VAL A 593 2426 1748 1105 604 24 -86 C

ATOM 2226 CG2 VAL A 593 -9.214 8.925 6.625 1.00 14.62 C ANISOU 2226 CG2 VAL A 593 2448 1881 1225 623 92 -55 C

ATOM 2227 C VAL A 593 -12.965 8.257 6.030 1.00 15.61 C

ANISOU 2227 C VAL A 593 2677 1954 1301 555 -14 -88 C

ATOM 2228 O VAL A 593 -13.354 7.211 5.489 1.00 10.15 O

ANISOU 2228 O VAL A 593 2041 1239 578 567 -31 -101 O

ATOM 2229 N LYS A 594 -13.708 8.929 6.899 1.00 11.72 N

ANISOU 2229 N LYS A 594 2147 1468 840 516 -34 -85 N

ATOM 2230 CA LYS A 594 -14.985 8.397 7.346 1.00 11.08 C

ANISOU 2230 CA LYS A 594 2083 1366 762 486 -76 -98 C

ATOM 2231 CB LYS A 594 -15.592 9.265 8.448 1.00 12.42 C

ANISOU 2231 CB LYS A 594 2203 1544 971 447 -88 -92 C

ATOM 2232 CG LYS A 594 -16.826 8.627 9.084 1.00 15.22 C

ANISOU 2232 CG LYS A 594 2569 1874 1341 417 -124 -103 C

ATOM 2233 CD LYS A 594 -17.498 9.569 10.072 1.00 12.85 C ANISOU 2233 CD LYS A 594 2223 1580 1081 380 -131 -95 C

ATOM 2234 CE LYS A 594 -18.757 8.929 10.660 1.00 16.73 C

ANISOU 2234 CE LYS A 594 2724 2043 1588 350 -161 -104 C

ATOM 2235 NZ LYS A 594 -18.441 7.699 11.446 1.00 14.51 N

ANISOU 2235 NZ LYS A 594 2463 1746 1306 358 -164 -114 N

ATOM 2236 C LYS A 594 -15.972 8.260 6.193 1.00 12.70 C

ANISOU 2236 C LYS A 594 2334 1553 937 483 -101 -106 C

ATOM 2237 O LYS A 594 -16.580 7.208 6.004 1.00 15.24 O

ANISOU 2237 O LYS A 594 2697 1848 1246 481 -128 -121 O

ATOM 2238 N VAL A 595 -16.141 9.325 5.424 1.00 11.50 N

ANISOU 2238 N VAL A 595 2177 1413 780 481 -93 -96 N

ATOM 2239 CA VAL A 595 -17.084 9.290 4.310 1.00 12.48 C

ANISOU 2239 CA VAL A 595 2344 1519 880 479 -120 -102 C

ATOM 2240 CB VAL A 595 -17.324 10.692 3.722 1.00 15.70 C

ANISOU 2240 CB VAL A 595 2733 1943 1289 473 -111 -87 C

ATOM 2241 CGI VAL A 595 -18.208 10.607 2.493 1.00 18.69 C

ANISOU 2241 CGI VAL A 595 3163 2303 1636 477 -141 -94 C

ATOM 2242 CG2 VAL A 595 -17.961 11.598 4.782 1.00 19.46 C

ANISOU 2242 CG2 VAL A 595 3151 2431 1813 434 -120 -79 C

ATOM 2243 C VAL A 595 -16.639 8.284 3.233 1.00 13.48 C

ANISOU 2243 C VAL A 595 2536 1628 957 517 -115 -112 C

ATOM 2244 0 VAL A 595 -17.461 7.555 2.686 1.00 10.52 O

ANISOU 2244 O VAL A 595 2207 1227 562 513 -151 -127 O

ATOM 2245 N MET A 596 -15.339 8.208 2.960 1.00 14.77 N

ANISOU 2245 N MET A 596 2704 1803 1104 553 -71 -105 N

ATOM 2246 CA MET A 596 -14.844 7.194 2.024 1.00 16.94 C

ANISOU 2246 CA MET A 596 3043 2059 1333 592 -61 -114 C

ATOM 2247 CB MET A 596 -13.354 7.399 1.718 1.00 14.65 C

ANISOU 2247 CB MET A 596 2743 1785 1038 632 -3 -100 C

ATOM 2248 CG MET A 596 -13.073 8.701 0.989 1.00 15.94 C

ANISOU 2248 CG MET A 596 2892 1965 1199 639 28 -82 C

ATOM 2249 SD MET A 596 -11.334 8.914 0.607 1.00 20.32 S

ANISOU 2249 SD MET A 596 3433 2536 1754 685 101 -64 S

ATOM 2250 CE MET A 596 -11.051 7.500 -0.458 1.00 38.21 C

ANISOU 2250 CE MET A 596 5788 4771 3961 731 108 -78 C

ATOM 2251 C MET A 596 -15.093 5.768 2.525 1.00 12.68 C

ANISOU 2251 C MET A 596 2533 1496 788 590 -87 -133 C

ATOM 2252 0 MET A 596 -15.371 4.866 1.737 1.00 12.57 O

ANISOU 2252 O MET A 596 2583 1456 736 606 -104 -147 O

ATOM 2253 N ALA A 597 -15.010 5.566 3.836 1.00 11.98 N

ANISOU 2253 N ALA A 597 2401 1414 736 572 -90 -133 N

ATOM 2254 CA ALA A 597 -15.189 4.231 4.401 1.00 14.54 C

ANISOU 2254 CA ALA A 597 2751 1715 1058 571 -110 -149 C

ATOM 2255 CB ALA A 597 -14.543 4.145 5.786 1.00 17.87 C

ANISOU 2255 CB ALA A 597 3124 2151 1514 567 -95 -143 C

ATOM 2256 C ALA A 597 -16.654 3.790 4.478 1.00 13.30 C ANISOU 2256 C ALA A 597 2613 1530 909 534 -161 -162 C

ATOM 2257 O ALA A 597 -16.952 2.600 4.365 1.00 15.50 O ANISOU 2257 O ALA A 597 2939 1780 1170 538 -181 -178 O

ATOM 2258 N GLU A 598 -17.560 4.744 4.663 1.00 9.78 N

ANISOU 2258 N GLU A 598 2133 1093 492 499 -181 -157 N

ATOM 2259 CA GLU A 598 -18.957 4.422 4.958 1.00 14.78 C ANISOU 2259 CA GLU A 598 2770 1703 1143 460 -226 -168 C

ATOM 2260 CB GLU A 598 -19.423 5.190 6.199 1.00 12.79 C ANISOU 2260 CB GLU A 598 2454 1466 942 424 -227 -158 C

ATOM 2261 CG GLU A 598 -18.587 4.840 7.435 1.00 11.94 C ANISOU 2261 CG GLU A 598 2320 1365 853 430 -203 -154 C

ATOM 2262 CD GLU A 598 -19.068 5.516 8.710 1.00 11.39 C ANISOU 2262 CD GLU A 598 2196 1305 829 395 -204 -146 C ATOM 2263 OEl GLU A 598 -20.046 6.289 8.656 1.00 16.80 O ANISOU 2263 OEl GLU A 598 2860 1991 1533 366 -221 -142 O ATOM 2264 OE2 GLU A 598 -18.461 5.270 9.774 1.00 15.75 O ANISOU 2264 OE2 GLU A 598 2729 1861 1396 399 -188 -143 O

ATOM 2265 C GLU A 598 -19.948 4.584 3.796 1.00 17.15 C

ANISOU 2265 C GLU A 598 3105 1988 1421 451 -262 -176 C

ATOM 2266 0 GLU A 598 -21.035 3.999 3.817 1.00 17.76 O ANISOU 2266 O GLU A 598 3202 2043 1504 425 -304 -191 O

ATOM 2267 N ALA A 599 -19.596 5.363 2.779 1.00 13.46 N

ANISOU 2267 N ALA A 599 2650 1535 929 473 -248 -167 N

ATOM 2268 CA ALA A 599 -20.474 5.418 1.611 1.00 14.62 C ANISOU 2268 CA ALA A 599 2841 1665 1047 470 -286 -176 C

ATOM 2269 CB ALA A 599 -20.097 6.564 0.684 1.00 12.32 C ANISOU 2269 CB ALA A 599 2552 1393 735 491 -264 -161 C

ATOM 2270 C ALA A 599 -20.385 4.073 0.884 1.00 17.94 C

ANISOU 2270 C ALA A 599 3337 2054 1424 492 -302 -196 C

ATOM 2271 O ALA A 599 -19.359 3.381 0.948 1.00 15.43 O ANISOU 2271 O ALA A 599 3041 1734 1087 523 -269 -196 O

ATOM 2272 N ASN A 600 -21.456 3.683 0.205 1.00 11.27 N

ANISOU 2272 N ASN A 600 2534 1185 563 477 -354 -212 N

ATOM 2273 CA ASN A 600 -21.391 2.457 -0.590 1.00 17.93 C ANISOU 2273 CA ASN A 600 3456 1996 1360 498 -371 -231 C

ATOM 2274 CB ASN A 600 -22.772 2.087 -1.141 1.00 17.92 C ANISOU 2274 CB ASN A 600 3489 1968 1353 470 -440 -252 C

ATOM 2275 CG ASN A 600 -23.789 1.835 -0.036 1.00 23.02 C ANISOU 2275 CG ASN A 600 4088 2607 2051 420 -471 -259 C ATOM 2276 ODl ASN A 600 -24.829 2.485 0.024 1.00 20.78 O ANISOU 2276 ODl ASN A 600 3770 2328 1797 388 -506 -258 O ATOM 2277 ND2 ASN A 600 -23.480 0.894 0.855 1.00 24.01 N ANISOU 2277 ND2 ASN A 600 4210 2721 2191 415 -456 -266 N

ATOM 2278 C ASN A 600 -20.374 2.607 -1.720 1.00 23.09 C

ANISOU 2278 C ASN A 600 4160 2653 1961 549 -336 -225 C

ATOM 2279 0 ASN A 600 -19.687 1.652 -2.085 1.00 19.79 O ANISOU 2279 O ASN A 600 3795 2217 1506 580 -319 -233 O

ATOM 2280 N HIS A 601 -20.274 3.821 -2.251 1.00 12.85 N

ANISOU 2280 N HIS A 601 2847 1377 660 557 -322 -209 N

ATOM 2281 CA HIS A 601 -19.346 4.141 -3.331 1.00 20.81 C

ANISOU 2281 CA HIS A 601 3899 2389 1618 603 -283 -200 C

ATOM 2282 CB HIS A 601 -20.047 4.081 -4.693 1.00 16.80 C

ANISOU 2282 CB HIS A 601 3466 1856 1060 614 -324 -212 C

ATOM 2283 CG HIS A 601 -20.765 2.792 -4.948 1.00 20.16 C

ANISOU 2283 CG HIS A 601 3950 2244 1465 604 -377 -238 C

ATOM 2284 CD2 HIS A 601 -22.078 2.471 -4.861 1.00 17.39 C

ANISOU 2284 CD2 HIS A 601 3601 1875 1131 564 -445 -256 C

ATOM 2285 ND1 HIS A 601 -20.114 1.640 -5.331 1.00 23.28 N

ANISOU 2285 ND1 HIS A 601 4411 2615 1820 635 -361 -250 N

ATOM 2286 CEl HIS A 601 -20.995 0.664 -5.473 1.00 29.62 C

ANISOU 2286 CEl HIS A 601 5256 3385 2612 615 -418 -275 C

ATOM 2287 NE2 HIS A 601 -22.195 1.143 -5.192 1.00 24.24 N

ANISOU 2287 NE2 HIS A 601 4536 2707 1968 571 -470 -279 N

ATOM 2288 C HIS A 601 -18.816 5.549 -3.115 1.00 18.54 C

ANISOU 2288 C HIS A 601 3553 2138 1354 606 -241 -175 C

ATOM 2289 O HIS A 601 -19.571 6.458 -2.760 1.00 17.37 O

ANISOU 2289 O HIS A 601 3357 2004 1240 574 -262 -168 O

ATOM 2290 N PHE A 602 -17.519 5.732 -3.321 1.00 13.17 N

ANISOU 2290 N PHE A 602 2876 1473 656 644 -180 -162 N

ATOM 2291 CA PHE A 602 -16.918 7.054 -3.233 1.00 18.37 C

ANISOU 2291 CA PHE A 602 3484 2163 1332 648 -136 -138 C

ATOM 2292 CB PHE A 602 -16.010 7.156 -2.008 1.00 17.70 C

ANISOU 2292 CB PHE A 602 3331 2104 1290 644 -95 -128 C

ATOM 2293 CG PHE A 602 -15.609 8.569 -1.670 1.00 8.60 C

ANISOU 2293 CG PHE A 602 2114 983 171 635 -61 -106 C

ATOM 2294 CDl PHE A 602 -16.278 9.267 -0.683 1.00 12.06 C

ANISOU 2294 CDl PHE A 602 2488 1437 656 593 -83 -101 C

ATOM 2295 CD2 PHE A 602 -14.565 9.184 -2.334 1.00 17.52 C

ANISOU 2295 CD2 PHE A 602 3247 2124 1284 669 -5 -88 C

ATOM 2296 CEl PHE A 602 -15.917 10.565 -0.365 1.00 18.47 C

ANISOU 2296 CEl PHE A 602 3245 2276 1498 584 -52 -82 C

ATOM 2297 CE2 PHE A 602 -14.194 10.480 -2.024 1.00 18.58 C

ANISOU 2297 CE2 PHE A 602 3324 2286 1452 659 27 -68 C

ATOM 2298 CZ PHE A 602 -14.873 11.170 -1.034 1.00 17.76 C

ANISOU 2298 CZ PHE A 602 3158 2197 1393 616 1 -65 C

ATOM 2299 C PHE A 602 -16.141 7.317 -4.512 1.00 17.02 C

ANISOU 2299 C PHE A 602 3371 1989 1107 695 -94 -130 C

ATOM 2300 O PHE A 602 -15.289 6.511 -4.898 1.00 18.52 O

ANISOU 2300 O PHE A 602 3603 2167 1267 732 -62 -133 O

ATOM 2301 N ILE A 603 -16.457 8.434 -5.172 1.00 14.24 N

ANISOU 2301 N ILE A 603 3021 1644 745 695 -93 -118 N

ATOM 2302 CA ILE A 603 -15.896 8.776 -6.483 1.00 16.96 C ANISOU 2302 CA ILE A 603 3427 1981 1037 738 -57 -108 C

ATOM 2303 CB ILE A 603 -16.992 8.856 -7.580 1.00 19.79 C

ANISOU 2303 CB ILE A 603 3855 2315 1351 738 -111 -119 C

ATOM 2304 CG2 ILE A 603 -16.383 9.244 -8.931 1.00 17.27 C

ANISOU 2304 CG2 ILE A 603 3606 1985 972 786 -70 -108 C

ATOM 2305 CGI ILE A 603 -17.734 7.523 -7.713 1.00 18.12 C

ANISOU 2305 CGI ILE A 603 3695 2070 1120 731 -171 -146 C

ATOM 2306 CD 1 ILE A 603 -18.823 7.318 -6.679 1.00 19.35 C

ANISOU 2306 CD 1 ILE A 603 3795 2228 1329 678 -229 -158 C

ATOM 2307 C ILE A 603 -15.186 10.125 -6.418 1.00 16.09 C ANISOU 2307 C ILE A 603 3264 1897 950 743 -0 -82 C

ATOM 2308 O ILE A 603 -15.798 11.147 -6.093 1.00 15.54 O

ANISOU 2308 O ILE A 603 3151 1845 910 714 -18 -73 O

ATOM 2309 N ASP A 604 -13.889 10.132 -6.709 1.00 18.17 N

ANISOU 2309 N ASP A 604 3533 2166 1204 781 68 -68 N

ATOM 2310 CA ASP A 604 -13.110 11.365 -6.634 1.00 19.20 C

ANISOU 2310 CA ASP A 604 3613 2321 1361 785 127 -43 C

ATOM 2311 CB ASP A 604 -11.651 11.060 -6.283 1.00 22.24 C

ANISOU 2311 CB ASP A 604 3967 2717 1767 812 193 -32 C

ATOM 2312 CG ASP A 604 -10.822 12.317 -6.092 1.00 29.15 C

ANISOU 2312 CG ASP A 604 4780 3617 2679 812 252 -7 C

ATOM 2313 OD1 ASP A 604 -11.376 13.433 -6.224 1.00 19.95 O

ANISOU 2313 ODl ASP A 604 3599 2460 1521 791 243 2 O

ATOM 2314 OD2 ASP A 604 -9.609 12.185 -5.811 1.00 26.38 O

ANISOU 2314 OD2 ASP A 604 4395 3276 2351 832 307 3 O

ATOM 2315 C ASP A 604 -13.192 12.125 -7.945 1.00 21.11 C

ANISOU 2315 C ASP A 604 3913 2551 1556 811 146 -32 C

ATOM 2316 O ASP A 604 -12.406 11.887 -8.864 1.00 16.64 O

ANISOU 2316 O ASP A 604 3403 1971 950 856 194 -26 O

ATOM 2317 N LEU A 605 -14.144 13.046 -8.043 1.00 12.18 N

ANISOU 2317 N LEU A 605 2771 1425 430 786 111 -28 N

ATOM 2318 CA LEU A 605 -14.300 13.804 -9.279 1.00 13.86 C

ANISOU 2318 CA LEU A 605 3043 1626 597 810 124 -18 C

ATOM 2319 CB LEU A 605 -15.707 14.405 -9.387 1.00 18.82 C

ANISOU 2319 CB LEU A 605 3674 2252 1223 781 57 -23 C

ATOM 2320 CG LEU A 605 -16.880 13.428 -9.529 1.00 18.01 C

ANISOU 2320 CG LEU A 605 3616 2129 1099 767 -26 -50 C

ATOM 2321 CD1 LEU A 605 -18.179 14.214 -9.690 1.00 14.29 C

ANISOU 2321 CD1 LEU A 605 3140 1658 633 740 -86 -50 C

ATOM 2322 CD2 LEU A 605 -16.671 12.474 -10.705 1.00 15.09 C

ANISOU 2322 CD2 LEU A 605 3351 1726 658 809 -28 -62 C

ATOM 2323 C LEU A 605 -13.247 14.909 -9.420 1.00 20.32 C

ANISOU 2323 C LEU A 605 3828 2461 1432 826 204 10 C

ATOM 2324 0 LEU A 605 -13.160 15.554 -10.463 1.00 19.67 O

ANISOU 2324 O LEU A 605 3796 2367 1310 853 232 22 O

ATOM 2325 N SER A 606 -12.459 15.145 -8.374 1.00 21.78 N ANISOU 2325 N SER A 606 3930 2671 1676 810 241 19 N ATOM 2326 CA SER A 606 -11.385 16.131 -8.489 1.00 21.05 C ANISOU 2326 CA SER A 606 3802 2593 1604 824 318 45 C ATOM 2327 CB SER A 606 -10.675 16.384 -7.145 1.00 14.14 C

ANISOU 2327 CB SER A 606 2825 1746 802 797 341 52 C ATOM 2328 OG SER A 606 -9.790 15.330 -6.801 1.00 22.63 O ANISOU 2328 OG SER A 606 3892 2821 1886 816 364 45 O

ATOM 2329 C SER A 606 -10.402 15.660 -9.556 1.00 23.47 C

ANISOU 2329 C SER A 606 4173 2879 1865 878 380 52 C

ATOM 2330 O SER A 606 -9.702 16.467 -10.153 1.00 19.29 O

ANISOU 2330 O SER A 606 3649 2349 1331 900 444 73 O

ATOM 2331 N GLN A 607 -10.392 14.353 -9.813 1.00 15.42 N

ANISOU 2331 N GLN A 607 3208 1840 812 900 361 34 N ATOM 2332 CA GLN A 607 -9.500 13.753 -10.816 1.00 23.82 C ANISOU 2332 CA GLN A 607 4341 2881 1830 954 418 39 C ATOM 2333 CB GLN A 607 -9.198 12.296 -10.446 1.00 30.58 C ANISOU 2333 CB GLN A 607 5210 3728 2682 966 405 21 C ATOM 2334 CG GLN A 607 -8.649 12.101 -9.046 1.00 44.29 C ANISOU 2334 CG GLN A 607 6847 5491 4488 941 410 21 C ATOM 2335 CD GLN A 607 -7.140 12.168 -8.997 1.00 65.63 C ANISOU 2335 CD GLN A 607 9514 8205 7220 972 494 41 C ATOM 2336 OEl GLN A 607 -6.536 13.138 -9.451 1.00 68.50 O ANISOU 2336 OEl GLN A 607 9863 8573 7591 984 553 63 O ATOM 2337 NE2 GLN A 607 -6.518 11.131 -8.441 1.00 79.79 N ANISOU 2337 NE2 GLN A 607 11290 9999 9030 984 501 33 N ATOM 2338 C GLN A 607 -10.082 13.793 -12.226 1.00 23.42 C

ANISOU 2338 C GLN A 607 4399 2799 1701 984 406 36 C ATOM 2339 O GLN A 607 -9.438 13.376 -13.191 1.00 24.01 O ANISOU 2339 O GLN A 607 4546 2850 1728 1032 454 41 O

ATOM 2340 N ILE A 608 -11.310 14.283 -12.337 1.00 24.25 N

ANISOU 2340 N ILE A 608 4518 2903 1794 957 341 29 N ATOM 2341 CA ILE A 608 -12.014 14.340 -13.609 1.00 29.55 C

ANISOU 2341 CA ILE A 608 5291 3544 2392 981 314 24 C ATOM 2342 CB ILE A 608 -13.226 13.383 -13.609 1.00 22.22 C

ANISOU 2342 CB ILE A 608 4406 2599 1438 964 218 -6 C ATOM 2343 CG2 ILE A 608 -13.879 13.329 -14.984 1.00 27.88 C ANISOU 2343 CG2 ILE A 608 5236 3282 2075 993 186 -13 C ATOM 2344 CGI ILE A 608 -12.794 11.982 -13.161 1.00 29.88 C ANISOU 2344 CGI ILE A 608 5379 3561 2412 971 216 -23 C ATOM 2345 CD1 ILE A 608 -13.899 10.932 -13.256 1.00 24.10 C ANISOU 2345 CD 1 ILE A 608 4700 2807 1651 956 128 -53 C

ATOM 2346 C ILE A 608 -12.481 15.776 -13.863 1.00 23.36 C

ANISOU 2346 C ILE A 608 4492 2770 1613 968 314 41 C

ATOM 2347 O ILE A 608 -13.635 16.118 -13.601 1.00 25.57 O

ANISOU 2347 O ILE A 608 4757 3055 1902 935 245 32 O ATOM 2348 N PRO A 609 -11.571 16.628 -14.358 1.00 28.83 N ANISOU 2348 N PRO A 609 5187 3465 2304 994 396 66 N

ATOM 2349 CD PRO A 609 -10.175 16.301 -14.687 1.00 34.42 C

ANISOU 2349 CD PRO A 609 5906 4165 3007 1034 486 80 C

ATOM 2350 CA PRO A 609 -11.855 18.061 -14.526 1.00 33.38 C

ANISOU 2350 CA PRO A 609 5742 4050 2890 981 410 86 C

ATOM 2351 CB PRO A 609 -10.520 18.630 -15.030 1.00 45.63 C

ANISOU 2351 CB PRO A 609 7296 5598 4442 1016 517 113 C

ATOM 2352 CG PRO A 609 -9.758 17.452 -15.552 1.00 38.10 C

ANISOU 2352 CG PRO A 609 6401 4622 3451 1059 551 106 C

ATOM 2353 C PRO A 609 -12.972 18.359 -15.527 1.00 36.68 C

ANISOU 2353 C PRO A 609 6245 4445 3246 993 355 80 C

ATOM 2354 0 PRO A 609 -13.711 19.329 -15.336 1.00 29.56 O

ANISOU 2354 O PRO A 609 5314 3556 2362 967 324 87 O

ATOM 2355 N CYS A 610 -13.098 17.547 -16.573 1.00 27.86 N

ANISOU 2355 N CYS A 610 5234 3295 2056 1032 340 68 N

ATOM 2356 CA CYS A 610 -14.137 17.781 -17.572 1.00 32.64 C

ANISOU 2356 CA CYS A 610 5927 3876 2598 1045 283 61 C

ATOM 2357 CB CYS A 610 -13.920 16.908 -18.810 1.00 25.83 C

ANISOU 2357 CB CYS A 610 5190 2973 1650 1098 291 52 C

ATOM 2358 SG CYS A 610 -15.208 17.134 -20.042 1.00 38.42 S

ANISOU 2358 SG CYS A 610 6898 4535 3163 1116 210 41 S

ATOM 2359 C CYS A 610 -15.532 17.533 -16.994 1.00 32.31 C

ANISOU 2359 C CYS A 610 5857 3843 2577 1001 175 39 C

ATOM 2360 O CYS A 610 -15.848 16.425 -16.567 1.00 25.67 O

ANISOU 2360 O CYS A 610 5012 2998 1742 987 126 16 O

ATOM 2361 N ASN A 611 -16.367 18.565 -16.980 1.00 26.99 N

ANISOU 2361 N ASN A 611 5162 3178 1914 981 139 47 N

ATOM 2362 CA ASN A 611 -17.726 18.414 -16.468 1.00 22.21 C

ANISOU 2362 CA ASN A 611 4527 2581 1333 941 40 28 C

ATOM 2363 CB ASN A 611 -18.407 19.773 -16.322 1.00 19.57 C

ANISOU 2363 CB ASN A 611 4151 2261 1023 920 24 44 C

ATOM 2364 CG ASN A 611 -17.816 20.593 -15.190 1.00 20.47 C

ANISOU 2364 CG ASN A 611 4156 2410 1213 889 79 63 C

ATOM 2365 ODl ASN A 611 -17.500 20.065 -14.121 1.00 27.47 O

ANISOU 2365 ODl ASN A 611 4972 3314 2151 861 84 55 O

ATOM 2366 ND2 ASN A 611 -17.664 21.888 -15.418 1.00 22.59 N

ANISOU 2366 ND2 ASN A 611 4413 2684 1484 894 120 87 N

ATOM 2367 C ASN A 611 -18.579 17.444 -17.289 1.00 27.22 C

ANISOU 2367 C ASN A 611 5254 3182 1906 956 -40 2 C

ATOM 2368 O ASN A 611 -19.495 16.811 -16.760 1.00 21.77 O

ANISOU 2368 O ASN A 611 4538 2493 1239 922 -118 -20 O

ATOM 2369 N GLY A 612 -18.267 17.324 -18.576 1.00 22.29 N

ANISOU 2369 N GLY A 612 4739 2527 1203 1006 -18 4 N

ATOM 2370 CA GLY A 612 -18.942 16.364 -19.433 1.00 23.41 C

ANISOU 2370 CA GLY A 612 4981 2634 1281 1025 -89 -21 C

ATOM 2371 C GLY A 612 -18.612 14.933 -19.043 1.00 28.11 C ANISOU 2371 C GLY A 612 5581 3221 1880 1021 -97 -43 C

ATOM 2372 0 GLY A 612 -19.498 14.101 -18.873 1.00 24.07 O

ANISOU 2372 O GLY A 612 5077 2698 1371 998 -180 -69 O

ATOM 2373 N LYS A 613 -17.326 14.640 -18.895 1.00 19.71 N

ANISOU 2373 N LYS A 613 4509 2160 820 1043 -8 -32 N

ATOM 2374 C A LYS A 613 -16.906 13.305 -18.489 1.00 20.06 C

ANISOU 2374 CA LYS A 613 4555 2197 870 1043 -7 -50 C

ATOM 2375 CB LYS A 613 -15.391 13.143 -18.629 1.00 27.47 C

ANISOU 2375 CB LYS A 613 5502 3134 1802 1082 101 -33 C

ATOM 2376 CG LYS A 613 -14.905 13.273 -20.075 1.00 39.76 C

ANISOU 2376 CG LYS A 613 7178 4656 3274 1142 149 -23 C

ATOM 2377 CD LYS A 613 -13.391 13.179 -20.181 1.00 49.14 C

ANISOU 2377 CD LYS A 613 8365 5843 4463 1180 263 -3 C

ATOM 2378 CE LYS A 613 -12.930 13.416 -21.615 1.00 60.64 C

ANISOU 2378 CE LYS A 613 9940 7263 5836 1241 317 10 C

ATOM 2379 NZ LYS A 613 -11.445 13.418 -21.726 1.00 63.78 N

ANISOU 2379 NZ LYS A 613 10331 7660 6243 1278 435 33 N

ATOM 2380 C LYS A 613 -17.365 12.991 -17.066 1.00 22.98 C

ANISOU 2380 C LYS A 613 4817 2596 1320 987 -49 -62 C

ATOM 2381 O LYS A 613 -17.774 11.871 -16.778 1.00 20.49 O

ANISOU 2381 O LYS A 613 4512 2268 1006 972 -100 -87 O

ATOM 2382 N ALA A 614 -17.316 13.983 -16.183 1.00 22.76 N

ANISOU 2382 N ALA A 614 4688 2602 1358 955 -27 -44 N

ATOM 2383 CA ALA A 614 -17.769 13.778 -14.806 1.00 16.40 C

ANISOU 2383 CA ALA A 614 3781 1823 627 902 -64 -53 C

ATOM 2384 CB ALA A 614 -17.391 14.967 -13.926 1.00 18.79 C

ANISOU 2384 CB ALA A 614 3982 2161 994 878 -17 -29 C

ATOM 2385 C ALA A 614 -19.278 13.506 -14.742 1.00 17.72 C

ANISOU 2385 C ALA A 614 3953 1979 800 869 -169 -75 C

ATOM 2386 O ALA A 614 -19.721 12.609 -14.022 1.00 20.72 O

ANISOU 2386 O ALA A 614 4303 2358 1211 839 -214 -95 O

ATOM 2387 N ALA A 615 -20.066 14.276 -15.493 1.00 24.33 N

ANISOU 2387 N ALA A 615 4827 2808 1609 874 -208 -71 N

ATOM 2388 CA ALA A 615 -21.507 14.032 -15.562 1.00 20.28 C

ANISOU 2388 CA ALA A 615 4322 2283 1101 847 -310 -91 C

ATOM 2389 CB ALA A 615 -22.209 15.133 -16.352 1.00 15.08 C

ANISOU 2389 CB ALA A 615 3694 1621 415 857 -340 -80 C

ATOM 2390 C ALA A 615 -21.816 12.664 -16.168 1.00 29.15 C

ANISOU 2390 C ALA A 615 5529 3370 2176 860 -363 -120 C

ATOM 2391 O ALA A 615 -22.761 11.992 -15.746 1.00 18.86 O

ANISOU 2391 O ALA A 615 4207 2061 900 825 -437 -142 O

ATOM 2392 N ASP A 616 -21.037 12.260 -17.171 1.00 24.72 N

ANISOU 2392 N ASP A 616 5065 2785 1545 909 -323 -120 N

ATOM 2393 CA ASP A 616 -21.203 10.937 -17.763 1.00 21.69 C

ANISOU 2393 CA ASP A 616 4768 2364 1110 925 -364 -147 C

ATOM 2394 CB ASP A 616 -20.191 10.704 -18.894 1.00 22.41 C ANISOU 2394 CB ASP A 616 4967 2429 1121 987 -301 -141 C

ATOM 2395 CG ASP A 616 -20.570 11.420 -20.172 1.00 30.14 C

ANISOU 2395 CG ASP A 616 6035 3386 2032 1020 -321 -134 C

ATOM 2396 OD1 ASP A 616 -19.774 11.382 -21.133 1.00 32.69 O ANISOU 2396 OD1 ASP A 616 6448 3687 2287 1073 -264 -126 O

ATOM 2397 OD2 ASP A 616 -21.665 12.019 -20.223 1.00 32.56 O

ANISOU 2397 OD2 ASP A 616 6322 3697 2351 997 -392 -137 O

ATOM 2398 C ASP A 616 -21.024 9.882 -16.692 1.00 20.63 C

ANISOU 2398 C ASP A 616 4579 2236 1025 896 -366 -162 C

ATOM 2399 O ASP A 616 -21.753 8.892 -16.652 1.00 23.60 O

ANISOU 2399 O ASP A 616 4978 2590 1398 877 -435 -188 O

ATOM 2400 N ARG A 617 -20.044 10.106 -15.820 1.00 21.45 N

ANISOU 2400 N ARG A 617 4609 2369 1174 892 -289 -144 N

ATOM 2401 CA ARG A 617 -19.743 9.174 -14.741 1.00 25.04 C

ANISOU 2401 CA ARG A 617 5008 2831 1674 868 -282 -155 C

ATOM 2402 CB ARG A 617 -18.488 9.629 -13.991 1.00 23.51 C

ANISOU 2402 CB ARG A 617 4744 2670 1520 876 -189 -131 C

ATOM 2403 CG ARG A 617 -18.105 8.735 -12.839 1.00 30.59 C

ANISOU 2403 CG ARG A 617 5583 3578 2464 854 -179 -139 C

ATOM 2404 CD ARG A 617 -17.708 7.335 -13.298 1.00 36.72 C

ANISOU 2404 CD ARG A 617 6438 4321 3192 883 -177 -158 C

ATOM 2405 NE ARG A 617 -17.277 6.557 -12.144 1.00 47.79 N

ANISOU 2405 NE ARG A 617 7782 5735 4642 865 -162 -164 N

ATOM 2406 CZ ARG A 617 -16.043 6.583 -11.659 1.00 32.56 C

ANISOU 2406 CZ ARG A 617 5815 3826 2732 885 -86 -148 C

ATOM 2407 NH1 ARG A 617 -15.115 7.325 -12.254 1.00 28.92 N

ANISOU 2407 NH1 ARG A 617 5365 3372 2251 921 -15 -125 N

ATOM 2408 NH2 ARG A 617 -15.736 5.860 -10.593 1.00 40.33 N

ANISOU 2408 NH2 ARG A 617 6747 4819 3757 868 -80 -154 N

ATOM 2409 C ARG A 617 -20.913 9.038 -13.769 1.00 26.29 C

ANISOU 2409 C ARG A 617 5093 3000 1896 810 -356 -168 C

ATOM 2410 O ARG A 617 -21.293 7.930 -13.375 1.00 23.17 O

ANISOU 2410 O ARG A 617 4702 2589 1511 791 -397 -191 O

ATOM 2411 N ILE A 618 -21.488 10.174 -13.384 1.00 18.01 N

ANISOU 2411 N ILE A 618 3978 1976 888 784 -370 -155 N

ATOM 2412 CA ILE A 618 -22.653 10.178 -12.510 1.00 16.07 C

ANISOU 2412 CA ILE A 618 3663 1740 703 731 -436 -165 C

ATOM 2413 CB ILE A 618 -23.068 11.623 -12.166 1.00 17.67 C

ANISOU 2413 CB ILE A 618 3797 1971 945 711 -432 -143 C

ATOM 2414 CG2 ILE A 618 -24.397 11.651 -11.425 1.00 17.76 C

ANISOU 2414 CG2 ILE A 618 3747 1988 1013 660 -505 -154 C

ATOM 2415 CGI ILE A 618 -21.978 12.297 -11.331 1.00 15.20 C

ANISOU 2415 CGI ILE A 618 3412 1691 671 712 -347 -119 C

ATOM 2416 CD1 ILE A 618 -22.229 13.797 -11.099 1.00 16.07 C

ANISOU 2416 CD1 ILE A 618 3465 1827 813 698 -332 -96 C

ATOM 2417 C ILE A 618 -23.841 9.445 -13.130 1.00 21.79 C ANISOU 2417 C ILE A 618 4446 2432 1400 720 -530 -192 C

ATOM 2418 O ILE A 618 -24.522 8.666 -12.464 1.00 25.71 O

ANISOU 2418 O ILE A 618 4914 2922 1934 683 -579 -211 O

ATOM 2419 N HIS A 619 -24.091 9.700 -14.410 1.00 22.97 N

ANISOU 2419 N HIS A 619 4682 2560 1486 751 -557 -194 N

ATOM 2420 C A HIS A 619 -25.204 9.065 -15.102 1.00 21.63 C

ANISOU 2420 CA HIS A 619 4573 2358 1286 743 -652 -221 C

ATOM 2421 CB HIS A 619 -25.426 9.710 -16.471 1.00 27.33 C

ANISOU 2421 CB HIS A 619 5382 3063 1939 780 -674 -216 C

ATOM 2422 CG HIS A 619 -26.406 8.974 -17.324 1.00 31.43 C

ANISOU 2422 CG HIS A 619 5982 3545 2416 780 -771 -245 C

ATOM 2423 CD2 HIS A 619 -27.759 8.931 -17.292 1.00 26.60 C

ANISOU 2423 CD2 HIS A 619 5349 2926 1830 744 -868 -261 C

ATOM 2424 ND1 HIS A 619 -26.019 8.136 -18.348 1.00 35.07 N

ANISOU 2424 ND1 HIS A 619 6559 3968 2798 819 -775 -261 N

ATOM 2425 CE1 HIS A 619 -27.093 7.621 -18.920 1.00 37.12 C

ANISOU 2425 CE1 HIS A 619 6869 4198 3035 806 -875 -287 C

ATOM 2426 NE2 HIS A 619 -28.161 8.083 -18.295 1.00 29.48 N

ANISOU 2426 NE2 HIS A 619 5818 3250 2133 760 -933 -288 N

ATOM 2427 C HIS A 619 -24.970 7.562 -15.266 1.00 22.98 C

ANISOU 2427 C HIS A 619 4808 2498 1427 750 -666 -246 C

ATOM 2428 O HIS A 619 -25.901 6.765 -15.178 1.00 26.00 O

ANISOU 2428 O HIS A 619 5198 2860 1819 720 -742 -271 O

ATOM 2429 N GLN A 620 -23.725 7.175 -15.503 1.00 25.93 N

ANISOU 2429 N GLN A 620 5224 2866 1763 789 -591 -239 N

ATOM 2430 CA GLN A 620 -23.408 5.759 -15.652 1.00 25.29 C

ANISOU 2430 CA GLN A 620 5204 2753 1650 801 -596 -262 C

ATOM 2431 CB GLN A 620 -21.965 5.573 -16.123 1.00 24.68 C

ANISOU 2431 CB GLN A 620 5182 2671 1524 855 -505 -249 C

ATOM 2432 CG GLN A 620 -21.715 4.230 -16.781 1.00 52.17 C

ANISOU 2432 CG GLN A 620 8766 6110 4945 882 -517 -272 C

ATOM 2433 CD GLN A 620 -22.687 3.955 -17.919 1.00 70.32 C ANISOU 2433 CD GLN A 620 11164 8370 7184 888 -603 -295 C

ATOM 2434 OEl GLN A 620 -22.658 4.625 -18.953 1.00 78.83 O ANISOU 2434 OEl GLN A 620 12306 9438 8206 922 -600 -286 O

ATOM 2435 NE2 GLN A 620 -23.557 2.968 -17.730 1.00 70.23 N ANISOU 2435 NE2 GLN A 620 11165 8335 7183 855 -681 -324 N

ATOM 2436 C GLN A 620 -23.656 5.015 -14.335 1.00 32.77 C

ANISOU 2436 C GLN A 620 6073 3711 2667 755 -609 -273 C

ATOM 2437 O GLN A 620 -24.050 3.848 -14.332 1.00 24.08 O

ANISOU 2437 O GLN A 620 5010 2582 1557 742 -655 -298 O

ATOM 2438 N ASP A 621 -23.444 5.699 -13.215 1.00 22.64 N

ANISOU 2438 N ASP A 621 4685 2467 1452 730 -571 -253 N

ATOM 2439 CA ASP A 621 -23.708 5.088 -11.911 1.00 19.32 C

ANISOU 2439 CA ASP A 621 4188 2055 1097 686 -581 -262 C

ATOM 2440 CB ASP A 621 -23.103 5.928 -10.787 1.00 21.14 C ANISOU 2440 CB ASP A 621 4317 2328 1389 673 -517 -236 C

ATOM 2441 CG ASP A 621 -21.605 5.797 -10.711 1.00 26.46 C ANISOU 2441 CG ASP A 621 4998 3010 2044 712 -430 -222 C ATOM 2442 ODl ASP A 621 -21.080 4.768 -11.187 1.00 20.94 O ANISOU 2442 ODl ASP A 621 4370 2286 1301 741 -418 -234 O ATOM 2443 OD2 ASP A 621 -20.957 6.716 -10.169 1.00 25.03 O ANISOU 2443 OD2 ASP A 621 4753 2863 1896 713 -373 -198 O

ATOM 2444 C ASP A 621 -25.203 4.875 -11.648 1.00 24.35 C

ANISOU 2444 C ASP A 621 4800 2681 1769 637 -673 -281 C

ATOM 2445 O ASP A 621 -25.576 4.182 -10.704 1.00 26.52 O

ANISOU 2445 O ASP A 621 5030 2955 2091 601 -692 -293 O

ATOM 2446 N GLY A 622 -26.054 5.488 -12.464 1.00 21.96 N ANISOU 2446 N GLY A 622 4525 2372 1446 636 -730 -284 N ATOM 2447 CA GLY A 622 -27.485 5.256 -12.371 1.00 18.69 C ANISOU 2447 CA GLY A 622 4095 1946 1062 593 -823 -303 C

ATOM 2448 C GLY A 622 -28.203 6.061 -11.292 1.00 21.35 C ANISOU 2448 C GLY A 622 4317 2312 1482 548 -833 -290 C

ATOM 2449 0 GLY A 622 -29.294 5.691 -10.852 1.00 19.05 O ANISOU 2449 O GLY A 622 3989 2011 1238 505 -895 -304 O

ATOM 2450 N ILE A 623 -27.603 7.171 -10.877 1.00 16.80 N

ANISOU 2450 N ILE A 623 3687 1771 925 557 -770 -262 N

ATOM 2451 CA ILE A 623 -28.167 8.007 -9.816 1.00 18.84 C

ANISOU 2451 CA ILE A 623 3840 2058 1259 519 -768 -246 C

ATOM 2452 CB ILE A 623 -27.319 9.289 -9.613 1.00 18.01 C

ANISOU 2452 CB ILE A 623 3696 1988 1158 539 -694 -215 C

ATOM 2453 CG2 ILE A 623 -27.919 10.173 -8.519 1.00 21.30 C ANISOU 2453 CG2 ILE A 623 4010 2432 1651 499 -693 -200 C

ATOM 2454 CGI ILE A 623 -25.860 8.926 -9.294 1.00 17.30 C ANISOU 2454 CGI ILE A 623 3613 1906 1054 565 -611 -207 C

ATOM 2455 CD 1 ILE A 623 -25.715 7.918 -8.178 1.00 13.10 C

ANISOU 2455 CD 1 ILE A 623 3043 1372 562 539 -602 -218 C

ATOM 2456 C ILE A 623 -29.632 8.411 -10.058 1.00 21.29 C

ANISOU 2456 C ILE A 623 4129 2361 1598 490 -852 -253 C

ATOM 2457 0 ILE A 623 -29.976 8.926 -11.126 1.00 17.15 O

ANISOU 2457 O ILE A 623 3654 1829 1032 511 -887 -252 O

ATOM 2458 N HIS A 624 -30.481 8.193 -9.053 1.00 15.86 N

ANISOU 2458 N HIS A 624 3367 1676 982 442 -881 -258 N

ATOM 2459 CA HIS A 624 -31.877 8.645 -9.086 1.00 18.41 C ANISOU 2459 CA HIS A 624 3650 1996 1348 411 -952 -260 C

ATOM 2460 CB HIS A 624 -32.767 7.711 -8.259 1.00 19.98 C

ANISOU 2460 CB HIS A 624 3805 2177 1609 362 -995 -279 C

ATOM 2461 CG HIS A 624 -32.801 6.303 -8.766 1.00 16.97 C ANISOU 2461 CG HIS A 624 3496 1758 1192 363 -1035 -309 C

ATOM 2462 CD2 HIS A 624 -33.434 5.756 -9.830 1.00 22.00 C ANISOU 2462 CD2 HIS A 624 4202 2363 1793 367 -1111 -332 C

ATOM 2463 ND1 HIS A 624 -32.115 5.274 -8.156 1.00 16.03 N ANISOU 2463 ND1 HIS A 624 3388 1630 1072 360 -996 -318 N

ATOM 2464 CE1 HIS A 624 -32.326 4.153 -8.823 1.00 19.56 C

ANISOU 2464 CE1 HIS A 624 3908 2041 1484 362 -1044 -345 C

ATOM 2465 NE2 HIS A 624 -33.121 4.419 -9.844 1.00 21.48 N

ANISOU 2465 NE2 HIS A 624 4187 2269 1704 366 -1115 -354 N

ATOM 2466 C HIS A 624 -32.032 10.070 -8.552 1.00 18.99 C

ANISOU 2466 C HIS A 624 3647 2104 1465 403 -922 -232 C

ATOM 2467 O HIS A 624 -32.706 10.901 -9.162 1.00 18.52 O

ANISOU 2467 O HIS A 624 3587 2046 1401 409 -961 -225 O

ATOM 2468 N ILE A 625 -31.433 10.337 -7.393 1.00 16.66 N

ANISOU 2468 N ILE A 625 3288 1833 1210 391 -855 -216 N

ATOM 2469 CA ILE A 625 -31.481 11.674 -6.799 1.00 14.04 C

ANISOU 2469 CA ILE A 625 2885 1532 918 383 -820 -189 C

ATOM 2470 CB ILE A 625 -32.224 11.655 -5.458 1.00 19.14 C

ANISOU 2470 CB ILE A 625 3442 2185 1647 336 -824 -187 C

ATOM 2471 CG2 ILE A 625 -32.181 13.032 -4.794 1.00 19.93 C

ANISOU 2471 CG2 ILE A 625 3473 2315 1784 330 -781 -159 C

ATOM 2472 CGI ILE A 625 -33.657 11.150 -5.654 1.00 17.98 C

ANISOU 2472 CGI ILE A 625 3285 2013 1532 305 -909 -205 C

ATOM 2473 CDl ILE A 625 -34.454 11.082 -4.367 1.00 24.80 C

ANISOU 2473 CDl ILE A 625 4063 2879 2481 258 -911 -202 C

ATOM 2474 C ILE A 625 -30.061 12.193 -6.577 1.00 16.01 C

ANISOU 2474 C ILE A 625 3135 1805 1142 412 -732 -170 C

ATOM 2475 O ILE A 625 -29.282 11.587 -5.836 1.00 16.02 O

ANISOU 2475 O ILE A 625 3124 1811 1153 408 -687 -173 O

ATOM 2476 N LEU A 626 -29.721 13.290 -7.242 1.00 14.74 N

ANISOU 2476 N LEU A 626 2991 1658 951 440 -709 -152 N

ATOM 2477 CA LEU A 626 -28.391 13.880 -7.112 1.00 16.33 C

ANISOU 2477 CA LEU A 626 3192 1882 1133 466 -626 -133 C

ATOM 2478 CB LEU A 626 -27.839 14.278 -8.483 1.00 17.22 C

ANISOU 2478 CB LEU A 626 3384 1987 1172 514 -613 -127 C

ATOM 2479 CG LEU A 626 -26.343 14.606 -8.539 1.00 10.97 C

ANISOU 2479 CG LEU A 626 2605 1209 353 546 -525 -111 C

ATOM 2480 CDl LEU A 626 -25.507 13.373 -8.232 1.00 9.08 C

ANISOU 2480 CDl LEU A 626 2385 960 104 553 -498 -125 C

ATOM 2481 CD2 LEU A 626 -25.962 15.202 -9.891 1.00 16.61 C ANISOU 2481 CD2 LEU A 626 3394 1915 1002 590 -511 -102 C

ATOM 2482 C LEU A 626 -28.511 15.097 -6.213 1.00 13.00 C

ANISOU 2482 C LEU A 626 2688 1488 765 446 -593 -110 C

ATOM 2483 O LEU A 626 -29.394 15.931 -6.411 1.00 14.98 O

ANISOU 2483 O LEU A 626 2917 1741 1032 437 -626 -101 O

ATOM 2484 N VAL A 627 -27.637 15.185 -5.217 1.00 11.95 N

ANISOU 2484 N VAL A 627 2509 1373 657 439 -531 -100 N

ATOM 2485 CA VAL A 627 -27.788 16.179 -4.163 1.00 14.11 C

ANISOU 2485 CA VAL A 627 2704 1670 988 413 -503 -81 C

ATOM 2486 CB VAL A 627 -27.828 15.513 -2.777 1.00 15.97 C ANISOU 2486 CB VAL A 627 2885 1907 1275 379 -494 -88 C

ATOM 2487 CGI VAL A 627 -27.959 16.562 -1.690 1.00 11.65 C

ANISOU 2487 CGI VAL A 627 2262 1382 781 355 -463 -69 C

ATOM 2488 CG2 VAL A 627 -28.988 14.507 -2.707 1.00 10.69 C

ANISOU 2488 CG2 VAL A 627 2220 1215 627 354 -561 -109 C

ATOM 2489 C VAL A 627 -26.671 17.215 -4.206 1.00 16.06 C

ANISOU 2489 C VAL A 627 2943 1939 1220 436 -433 -59 C

ATOM 2490 O VAL A 627 -25.493 16.886 -4.070 1.00 14.02 O

ANISOU 2490 O VAL A 627 2696 1686 945 452 -382 -57 O

ATOM 2491 N ASN A 628 -27.060 18.468 -4.406 1.00 14.33 N

ANISOU 2491 N ASN A 628 2704 1731 1010 436 -430 -41 N

ATOM 2492 CA ASN A 628 -26.114 19.567 -4.520 1.00 13.30 C

ANISOU 2492 CA ASN A 628 2567 1619 868 455 -366 -19 C

ATOM 2493 CB ASN A 628 -26.692 20.635 -5.449 1.00 17.52 C

ANISOU 2493 CB ASN A 628 3125 2151 1380 471 -383 -5 C

ATOM 2494 CG ASN A 628 -25.681 21.692 -5.821 1.00 24.44 C

ANISOU 2494 CG ASN A 628 4012 3041 2234 496 -317 17 C

ATOM 2495 ODl ASN A 628 -24.712 21.914 -5.102 1.00 12.26 O

ANISOU 2495 ODl ASN A 628 2432 1513 712 491 -258 25 O

ATOM 2496 ND2 ASN A 628 -25.911 22.362 -6.949 1.00 22.23 N

ANISOU 2496 ND2 ASN A 628 3780 2753 1913 523 -326 26 N

ATOM 2497 C ASN A 628 -25.812 20.153 -3.143 1.00 14.54 C

ANISOU 2497 C ASN A 628 2646 1796 1081 427 -325 -6 C

ATOM 2498 O ASN A 628 -26.663 20.814 -2.544 1.00 14.61 O

ANISOU 2498 O ASN A 628 2608 1811 1133 401 -342 2 O

ATOM 2499 N MET A 629 -24.612 19.890 -2.629 1.00 13.27 N

ANISOU 2499 N MET A 629 2474 1645 922 432 -272 -4 N

ATOM 2500 CA MET A 629 -24.245 20.361 -1.296 1.00 6.35 C

ANISOU 2500 CA MET A 629 1529 787 96 406 -236 5 C

ATOM 2501 CB MET A 629 -23.498 19.267 -0.513 1.00 5.81 C

ANISOU 2501 CB MET A 629 1450 718 38 401 -220 -7 C

ATOM 2502 CG MET A 629 -24.338 17.987 -0.323 1.00 9.99 C

ANISOU 2502 CG MET A 629 1994 1229 573 387 -274 -29 C

ATOM 2503 SD MET A 629 -23.403 16.579 0.308 1.00 15.16 S

ANISOU 2503 SD MET A 629 2655 1878 1227 391 -255 -45 S

ATOM 2504 CE MET A 629 -22.802 17.279 1.846 1.00 17.33 C

ANISOU 2504 CE MET A 629 2855 2174 1553 368 -210 -31 C

ATOM 2505 C MET A 629 -23.432 21.667 -1.313 1.00 7.00 C

ANISOU 2505 C MET A 629 1592 887 180 416 -178 28 C

ATOM 2506 O MET A 629 -23.044 22.160 -0.267 1.00 13.06 O

ANISOU 2506 O MET A 629 2307 1669 986 396 -147 36 O

ATOM 2507 N ASN A 630 -23.163 22.205 -2.501 1.00 8.27 N

ANISOU 2507 N ASN A 630 1799 1045 299 446 -164 37 N

ATOM 2508 CA ASN A 630 -22.363 23.431 -2.618 1.00 10.61 C

ANISOU 2508 CA ASN A 630 2081 1355 595 456 -106 59 C

ATOM 2509 CB ASN A 630 -21.298 23.281 -3.711 1.00 10.17 C ANISOU 2509 CB ASN A 630 2081 1294 489 496 -65 63 C

ATOM 2510 CG ASN A 630 -20.024 22.632 -3.207 1.00 17.25 C

ANISOU 2510 CG ASN A 630 2962 2198 1394 502 -21 59 C

ATOM 2511 OD1 ASN A 630 -19.879 21.418 -3.265 1.00 16.73 O

ANISOU 2511 OD1 ASN A 630 2920 2122 1313 511 -38 42 O

ATOM 2512 ND2 ASN A 630 -19.085 23.448 -2.726 1.00 14.54 N

ANISOU 2512 ND2 ASN A 630 2578 1871 1077 497 35 75 N

ATOM 2513 C ASN A 630 -23.153 24.696 -2.931 1.00 13.44 C

ANISOU 2513 C ASN A 630 2434 1715 958 452 -115 75 C

ATOM 2514 O ASN A 630 -22.889 25.750 -2.365 1.00 8.88 O

ANISOU 2514 O ASN A 630 1814 1149 409 439 -79 91 O

ATOM 2515 N GLY A 631 -24.097 24.610 -3.861 1.00 17.68 N

ANISOU 2515 N GLY A 631 3014 2237 1465 465 -164 70 N

ATOM 2516 CA GLY A 631 -24.656 25.830 -4.423 1.00 15.77 C

ANISOU 2516 CA GLY A 631 2780 1995 1215 473 -167 88 C

ATOM 2517 C GLY A 631 -23.519 26.740 -4.886 1.00 19.78 C

ANISOU 2517 C GLY A 631 3304 2509 1702 496 -97 107 C

ATOM 2518 O GLY A 631 -22.524 26.274 -5.442 1.00 14.92 O

ANISOU 2518 O GLY A 631 2726 1890 1053 521 -62 105 O

ATOM 2519 N TYR A 632 -23.650 28.038 -4.641 1.00 7.75 N

ANISOU 2519 N TYR A 632 1751 994 199 487 -72 126 N

ATOM 2520 CA TYR A 632 -22.621 28.977 -5.059 1.00 13.83 C

ANISOU 2520 CA TYR A 632 2534 1769 954 505 -4 146 C

ATOM 2521 CB TYR A 632 -23.267 30.278 -5.552 1.00 19.41 C

ANISOU 2521 CB TYR A 632 3251 2472 1653 512 -5 165 C

ATOM 2522 CG TYR A 632 -24.312 29.975 -6.594 1.00 20.61 C

ANISOU 2522 CG TYR A 632 3460 2608 1764 534 -67 158 C

ATOM 2523 CDl TYR A 632 -23.957 29.343 -7.787 1.00 15.76 C

ANISOU 2523 CDl TYR A 632 2921 1978 1090 571 -70 151 C

ATOM 2524 CE1 TYR A 632 -24.910 29.037 -8.745 1.00 23.55 C

ANISOU 2524 CE1 TYR A 632 3964 2948 2037 592 -133 143 C

ATOM 2525 CD2 TYR A 632 -25.650 30.278 -6.384 1.00 13.68 C

ANISOU 2525 CD2 TYR A 632 2561 1728 908 519 -124 158 C

ATOM 2526 CE2 TYR A 632 -26.613 29.976 -7.346 1.00 12.00 C

ANISOU 2526 CE2 TYR A 632 2399 1500 661 540 -188 151 C

ATOM 2527 CZ TYR A 632 -26.230 29.360 -8.521 1.00 11.08 C

ANISOU 2527 CZ TYR A 632 2359 1369 483 575 -194 143 C

ATOM 2528 OH TYR A 632 -27.168 29.038 -9.471 1.00 13.64 O

ANISOU 2528 OH TYR A 632 2737 1676 771 595 -262 134 O

ATOM 2529 C TYR A 632 -21.560 29.207 -3.979 1.00 8.63 C

ANISOU 2529 C TYR A 632 1816 1125 337 483 51 151 C

ATOM 2530 O TYR A 632 -21.360 30.321 -3.528 1.00 17.62 O

ANISOU 2530 O TYR A 632 2921 2272 1502 469 86 167 O

ATOM 2531 N THR A 633 -20.868 28.126 -3.604 1.00 16.28 N

ANISOU 2531 N THR A 633 2778 2097 1310 482 58 136 N

ATOM 2532 CA THR A 633 -19.751 28.183 -2.658 1.00 9.74 C ANISOU 2532 CA THR A 633 1899 1283 518 466 106 139 C

ATOM 2533 CB THR A 633 -20.061 27.427 -1.355 1.00 17.46 C

ANISOU 2533 CB THR A 633 2828 2267 1537 434 74 123 C ATOM 2534 OGl THR A 633 -20.451 26.084 -1.671 1.00 12.16 O

ANISOU 2534 OGl THR A 633 2191 1586 842 444 30 104 O

ATOM 2535 CG2 THR A 633 -21.172 28.127 -0.536 1.00 9.43 C

ANISOU 2535 CG2 THR A 633 1771 1253 557 402 44 128 C

ATOM 2536 C THR A 633 -18.477 27.597 -3.243 1.00 11.47 C

ANISOU 2536 C THR A 633 2146 1500 711 494 150 138 C

ATOM 2537 O THR A 633 -18.505 26.860 -4.241 1.00 16.35 O

ANISOU 2537 O THR A 633 2826 2105 1283 525 137 130 O

ATOM 2538 N LYS A 634 -17.353 27.920 -2.608 1.00 21.01 N

ANISOU 2538 N LYS A 634 3311 2720 1951 485 201 145 N

ATOM 2539 CA LYS A 634 -16.047 27.548 -3.134 1.00 17.82 C

ANISOU 2539 CA LYS A 634 2924 2316 1531 512 253 148 C

ATOM 2540 CB LYS A 634 -14.939 27.908 -2.139 1.00 15.78 C

ANISOU 2540 CB LYS A 634 2601 2074 1323 493 298 154 C

ATOM 2541 CG LYS A 634 -13.550 27.530 -2.628 1.00 27.19 C

ANISOU 2541 CG LYS A 634 4054 3518 2760 520 354 159 C

ATOM 2542 CD LYS A 634 -12.472 28.327 -1.910 1.00 43.06 C

ANISOU 2542 CD LYS A 634 6001 5541 4820 502 405 171 C

ATOM 2543 CE LYS A 634 -11.773 27.496 -0.852 1.00 45.12 C

ANISOU 2543 CE LYS A 634 6212 5814 5116 490 399 158 C

ATOM 2544 NZ LYS A 634 -10.922 26.431 -1.452 1.00 41.39 N

ANISOU 2544 NZ LYS A 634 5766 5337 4622 525 422 154 N

ATOM 2545 C LYS A 634 -15.960 26.063 -3.486 1.00 22.00 C

ANISOU 2545 C LYS A 634 3492 2836 2030 534 229 130 C

ATOM 2546 O LYS A 634 -16.334 25.207 -2.693 1.00 14.04 O

ANISOU 2546 O LYS A 634 2463 1832 1041 516 189 113 O

ATOM 2547 N GLY A 635 -15.453 25.766 -4.676 1.00 16.52 N

ANISOU 2547 N GLY A 635 2859 2130 1290 573 257 133 N

ATOM 2548 CA GLY A 635 -15.239 24.391 -5.081 1.00 18.56 C ANISOU 2548 CA GLY A 635 3158 2376 1516 597 242 117 C

ATOM 2549 C GLY A 635 -16.411 23.794 -5.837 1.00 16.79 C

ANISOU 2549 C GLY A 635 2998 2135 1247 608 180 103 C

ATOM 2550 O GLY A 635 -16.338 22.662 -6.306 1.00 16.90 O

ANISOU 2550 O GLY A 635 3059 2136 1228 630 163 88 O

ATOM 2551 N ALA A 636 -17.495 24.553 -5.960 1.00 12.43 N

ANISOU 2551 N ALA A 636 2449 1581 694 595 143 107 N

ATOM 2552 CA ALA A 636 -18.678 24.062 -6.661 1.00 14.47 C

ANISOU 2552 CA ALA A 636 2763 1822 914 603 77 94 C

ATOM 2553 CB ALA A 636 -19.803 25.082 -6.596 1.00 14.67 C

ANISOU 2553 CB ALA A 636 2771 1849 952 584 43 103 C

ATOM 2554 C ALA A 636 -18.410 23.729 -8.117 1.00 19.60 C

ANISOU 2554 C ALA A 636 3502 2450 1495 649 89 94 C

ATOM 2555 O ALA A 636 -17.585 24.368 -8.785 1.00 15.24 O ANISOU 2555 O ALA A 636 2973 1894 921 675 150 112 O

ATOM 2556 N ARG A 637 -19.161 22.753 -8.614 1.00 14.22 N

ANISOU 2556 N ARG A 637 2872 1752 780 658 29 75 N

ATOM 2557 CA ARG A 637 -19.189 22.445 -10.040 1.00 18.99 C

ANISOU 2557 CA ARG A 637 3572 2331 1313 700 23 72 C

ATOM 2558 CB ARG A 637 -18.330 21.224 -10.358 1.00 18.39 C

ANISOU 2558 CB ARG A 637 3538 2243 1208 727 46 60 C

ATOM 2559 CG ARG A 637 -16.838 21.502 -10.231 1.00 19.64 C

ANISOU 2559 CG ARG A 637 3673 2411 1379 743 137 77 C

ATOM 2560 CD ARG A 637 -16.018 20.228 -10.336 1.00 19.92 C

ANISOU 2560 CD ARG A 637 3736 2437 1397 766 157 65 C

ATOM 2561 NE ARG A 637 -16.165 19.591 -11.642 1.00 21.52 N

ANISOU 2561 NE ARG A 637 4042 2609 1526 807 144 56 N

ATOM 2562 CZ ARG A 637 -15.524 18.483 -12.002 1.00 19.26 C

ANISOU 2562 CZ ARG A 637 3801 2308 1209 835 162 46 C

ATOM 2563 NHl ARG A 637 -14.685 17.905 -11.159 1.00 18.99 N

ANISOU 2563 NHl ARG A 637 3714 2287 1214 827 194 43 N

ATOM 2564 NH2 ARG A 637 -15.721 17.964 -13.205 1.00 19.27 N

ANISOU 2564 NH2 ARG A 637 3903 2279 1140 872 147 37 N

ATOM 2565 C ARG A 637 -20.644 22.241 -10.452 1.00 21.30 C

ANISOU 2565 C ARG A 637 3897 2609 1585 693 -64 58 C

ATOM 2566 0 ARG A 637 -21.074 21.143 -10.784 1.00 16.89 O

ANISOU 2566 O ARG A 637 3382 2034 1000 700 -114 37 O

ATOM 2567 N ASN A 638 -21.404 23.328 -10.408 1.00 14.36 N

ANISOU 2567 N ASN A 638 2996 1737 723 680 -83 70 N

ATOM 2568 CA ASN A 638 -22.825 23.266 -10.682 1.00 13.46 C

ANISOU 2568 CA ASN A 638 2900 1614 603 670 -167 60 C

ATOM 2569 CB ASN A 638 -23.498 24.559 -10.216 1.00 16.88 C

ANISOU 2569 CB ASN A 638 3278 2061 1075 647 -173 77 C

ATOM 2570 CG ASN A 638 -23.394 24.740 -8.712 1.00 15.32 C

ANISOU 2570 CG ASN A 638 2985 1887 951 605 -155 79 C

ATOM 2571 OD1 ASN A 638 -23.735 23.838 -7.954 1.00 16.72 O

ANISOU 2571 OD1 ASN A 638 3129 2066 1158 579 -189 62 O

ATOM 2572 ND2 ASN A 638 -22.913 25.897 -8.274 1.00 16.62 N ANISOU 2572 ND2 ASN A 638 3106 2067 1142 596 -101 101 N

ATOM 2573 C ASN A 638 -23.121 22.944 -12.141 1.00 18.87 C

ANISOU 2573 C ASN A 638 3687 2271 1212 710 -199 53 C

ATOM 2574 0 ASN A 638 -24.245 22.579 -12.481 1.00 19.89 O

ANISOU 2574 O ASN A 638 3841 2387 1329 706 -278 38 O

ATOM 2575 N GLU A 639 -22.100 23.051 -12.990 1.00 14.47 N

ANISOU 2575 N GLU A 639 3189 1702 605 751 -138 63 N

ATOM 2576 CA GLU A 639 -22.189 22.570 -14.362 1.00 15.05 C

ANISOU 2576 CA GLU A 639 3371 1746 600 793 -160 55 C

ATOM 2577 CB GLU A 639 -20.833 22.700 -15.066 1.00 26.61 C

ANISOU 2577 CB GLU A 639 4888 3201 2022 835 -71 70 C

ATOM 2578 CG GLU A 639 -20.425 24.123 -15.418 1.00 23.49 C ANISOU 2578 CG GLU A 639 4493 2811 1622 851 -10 99 C ATOM 2579 CD GLU A 639 -20.014 24.955 -14.209 1.00 32.83 C

ANISOU 2579 CD GLU A 639 5569 4024 2879 814 37 115 C ATOM 2580 OEl GLU A 639 -19.959 26.195 -14.353 1.00 42.83 O ANISOU 2580 OEl GLU A 639 6826 5296 4152 817 72 137 O ATOM 2581 OE2 GLU A 639 -19.749 24.386 -13.124 1.00 22.37 O ANISOU 2581 OE2 GLU A 639 4175 2717 1607 783 39 105 O

ATOM 2582 C GLU A 639 -22.643 21.108 -14.386 1.00 20.91 C

ANISOU 2582 C GLU A 639 4143 2473 1330 788 -224 25 C

ATOM 2583 O GLU A 639 -23.381 20.694 -15.283 1.00 18.78 O

ANISOU 2583 O GLU A 639 3945 2178 1011 805 -287 11 O

ATOM 2584 N LEU A 640 -22.201 20.331 -13.399 1.00 19.90 N

ANISOU 2584 N LEU A 640 3960 2358 1245 763 -209 15 N ATOM 2585 CA LEU A 640 -22.581 18.920 -13.303 1.00 16.20 C

ANISOU 2585 CA LEU A 640 3513 1873 771 754 -264 -13 C ATOM 2586 CB LEU A 640 -21.932 18.250 -12.088 1.00 14.67 C

ANISOU 2586 CB LEU A 640 3250 1696 629 729 -232 -19 C ATOM 2587 CG LEU A 640 -20.407 18.178 -12.078 1.00 18.03 C

ANISOU 2587 CG LEU A 640 3679 2128 1043 755 -141 -6 C ATOM 2588 CDl LEU A 640 -19.887 17.781 -10.699 1.00 18.00 C

ANISOU 2588 CDl LEU A 640 3590 2146 1103 724 -116 -9 C ATOM 2589 CD2 LEU A 640 -19.916 17.212 -13.155 1.00 21.19 C ANISOU 2589 CD2 LEU A 640 4179 2499 1374 798 -133 -18 C

ATOM 2590 C LEU A 640 -24.087 18.777 -13.212 1.00 17.03 C

ANISOU 2590 C LEU A 640 3606 1971 893 726 -360 -29 C

ATOM 2591 O LEU A 640 -24.667 17.905 -13.842 1.00 21.54 O

ANISOU 2591 O LEU A 640 4238 2517 1428 734 -422 -51 O

ATOM 2592 N PHE A 641 -24.718 19.640 -12.421 1.00 19.50 N

ANISOU 2592 N PHE A 641 3841 2306 1263 693 -373 -18 N ATOM 2593 CA PHE A 641 -26.170 19.644 -12.296 1.00 18.39 C

ANISOU 2593 CA PHE A 641 3680 2162 1147 666 -461 -29 C ATOM 2594 CB PHE A 641 -26.593 20.325 -10.991 1.00 17.73 C

ANISOU 2594 CB PHE A 641 3490 2105 1142 623 -455 -18 C

ATOM 2595 CG PHE A 641 -26.188 19.564 -9.757 1.00 19.33 C

ANISOU 2595 CG PHE A 641 3632 2319 1394 592 -433 -27 C ATOM 2596 CDl PHE A 641 -27.079 18.712 -9.130 1.00 13.76 C

ANISOU 2596 CDl PHE A 641 2895 1607 726 558 -493 -46 C ATOM 2597 CD2 PHE A 641 -24.906 19.688 -9.238 1.00 16.35 C ANISOU 2597 CD2 PHE A 641 3230 1957 1027 597 -353 -15 C

ATOM 2598 CE1 PHE A 641 -26.705 17.997 -7.976 1.00 10.93 C

ANISOU 2598 CE1 PHE A 641 2486 1257 411 531 -471 -54 C

ATOM 2599 CE2 PHE A 641 -24.529 18.992 -8.101 1.00 17.45 C ANISOU 2599 CE2 PHE A 641 3316 2105 1209 572 -336 -24 C

ATOM 2600 CZ PHE A 641 -25.427 18.133 -7.477 1.00 14.87 C

ANISOU 2600 CZ PHE A 641 2963 1771 914 540 -394 -43 C

ATOM 2601 C PHE A 641 -26.869 20.277 -13.508 1.00 19.50 C ANISOU 2601 C PHE A 641 3886 2286 1238 694 -505 -24 C

ATOM 2602 O PHE A 641 -27.965 19.861 -13.883 1.00 15.70 O

ANISOU 2602 O PHE A 641 3426 1788 750 686 -590 -41 O

ATOM 2603 N ALA A 642 -26.233 21.269 -14.127 1.00 15.26 N

ANISOU 2603 N ALA A 642 3381 1752 666 726 -449 -2 N

ATOM 2604 CA ALA A 642 -26.784 21.863 -15.347 1.00 18.06 C

ANISOU 2604 CA ALA A 642 3809 2088 965 759 -486 4 C

ATOM 2605 CB ALA A 642 -25.942 23.060 -15.798 1.00 20.15 C

ANISOU 2605 CB ALA A 642 4095 2358 1202 790 -405 33 C

ATOM 2606 C ALA A 642 -26.899 20.830 -16.470 1.00 24.43 C

ANISOU 2606 C ALA A 642 4721 2861 1700 790 -533 -19 C

ATOM 2607 O ALA A 642 -27.758 20.951 -17.353 1.00 16.16 O

ANISOU 2607 O ALA A 642 3731 1795 614 806 -602 -25 O

ATOM 2608 N LEU A 643 -26.032 19.821 -16.439 1.00 15.38 N

ANISOU 2608 N LEU A 643 3602 1706 535 799 -497 -30 N

ATOM 2609 CA LEU A 643 -26.084 18.731 -17.418 1.00 19.62 C

ANISOU 2609 CA LEU A 643 4240 2209 1007 826 -538 -53 C

ATOM 2610 CB LEU A 643 -24.737 18.008 -17.506 1.00 19.72 C

ANISOU 2610 CB LEU A 643 4287 2214 990 851 -461 -54 C

ATOM 2611 CG LEU A 643 -23.658 18.763 -18.286 1.00 22.35 C

ANISOU 2611 CG LEU A 643 4676 2543 1272 898 -374 -30 C

ATOM 2612 CDl LEU A 643 -22.266 18.258 -17.921 1.00 24.98 C

ANISOU 2612 CDl LEU A 643 4998 2883 1610 909 -284 -24 C

ATOM 2613 CD2 LEU A 643 -23.903 18.653 -19.789 1.00 23.85 C

ANISOU 2613 CD2 LEU A 643 4995 2696 1371 945 -406 -36 C

ATOM 2614 C LEU A 643 -27.214 17.737 -17.124 1.00 25.73 C

ANISOU 2614 C LEU A 643 4999 2972 1806 792 -637 -83 C

ATOM 2615 O LEU A 643 -27.545 16.902 -17.966 1.00 23.26 O

ANISOU 2615 O LEU A 643 4769 2629 1440 810 -693 -104 O

ATOM 2616 N ARG A 644 -27.805 17.843 -15.934 1.00 22.25 N

ANISOU 2616 N ARG A 644 4455 2555 1445 744 -658 -83 N

ATOM 2617 CA ARG A 644 -28.930 16.986 -15.533 1.00 18.34 C

ANISOU 2617 CA ARG A 644 3932 2051 986 706 -747 -108 C

ATOM 2618 CB ARG A 644 -30.210 17.426 -16.250 1.00 21.80 C

ANISOU 2618 CB ARG A 644 4393 2476 1413 708 -837 -113 C

ATOM 2619 CG ARG A 644 -30.797 18.733 -15.736 1.00 27.84 C

ANISOU 2619 CG ARG A 644 5080 3266 2231 690 -836 -90 C

ATOM 2620 CD ARG A 644 -31.991 19.160 -16.581 1.00 42.42 C

ANISOU 2620 CD ARG A 644 6959 5098 4059 700 -925 -94 C

ATOM 2621 NE ARG A 644 -32.444 20.511 -16.260 1.00 56.29 N

ANISOU 2621 NE ARG A 644 8656 6877 5856 694 -916 -68 N

ATOM 2622 CZ ARG A 644 -33.508 21.092 -16.808 1.00 60.34 C

ANISOU 2622 CZ ARG A 644 9176 7382 6366 700 -987 -66 C

ATOM 2623 NHl ARG A 644 -34.234 20.438 -17.707 1.00 73.47 N ANISOU 2623 NHl ARG A 644 10905 9018 7992 712 -1078 -88 N

ATOM 2624 NH2 ARG A 644 -33.849 22.326 -16.458 1.00 44.29 N ANISOU 2624 NH2 ARG A 644 7088 5371 4371 696 -970 -41 N

ATOM 2625 C ARG A 644 -28.712 15.475 -15.745 1.00 19.38 C

ANISOU 2625 C ARG A 644 4119 2157 1089 709 -770 -137 C

ATOM 2626 O ARG A 644 -29.494 14.823 -16.448 1.00 23.65 O

ANISOU 2626 O ARG A 644 4718 2670 1599 711 -851 -159 O

ATOM 2627 N PRO A 645 -27.657 14.910 -15.133 1.00 20.79 N

ANISOU 2627 N PRO A 645 4279 2343 1278 708 -700 -136 N

ATOM 2628 CD PRO A 645 -26.602 15.611 -14.381 1.00 22.94 C

ANISOU 2628 CD PRO A 645 4490 2644 1581 709 -603 -111 C

ATOM 2629 CA PRO A 645 -27.396 13.466 -15.237 1.00 21.44 C

ANISOU 2629 CA PRO A 645 4409 2400 1336 710 -715 -161 C

ATOM 2630 CB PRO A 645 -25.990 13.316 -14.636 1.00 19.44 C

ANISOU 2630 CB PRO A 645 4131 2163 1093 722 -615 -149 C

ATOM 2631 CG PRO A 645 -25.857 14.485 -13.709 1.00 16.97 C

ANISOU 2631 CG PRO A 645 3721 1887 841 700 -569 -123 C

ATOM 2632 C PRO A 645 -28.388 12.609 -14.449 1.00 21.58 C

ANISOU 2632 C PRO A 645 4376 2414 1408 661 -785 -184 C

ATOM 2633 O PRO A 645 -28.386 11.382 -14.595 1.00 23.27 O

ANISOU 2633 O PRO A 645 4636 2604 1603 659 -813 -208 O

ATOM 2634 N ALA A 646 -29.211 13.243 -13.616 1.00 15.91 N

ANISOU 2634 N ALA A 646 3567 1717 761 622 -810 -176 N

ATOM 2635 CA ALA A 646 -30.166 12.521 -12.780 1.00 19.63 C

ANISOU 2635 CA ALA A 646 3980 2183 1294 573 -867 -194 C

ATOM 2636 CB ALA A 646 -29.714 12.537 -11.314 1.00 26.81 C

ANISOU 2636 CB ALA A 646 4796 3120 2272 542 -808 -184 C

ATOM 2637 C ALA A 646 -31.560 13.122 -12.913 1.00 21.92 C

ANISOU 2637 C ALA A 646 4237 2473 1619 551 -946 -195 C

ATOM 2638 O ALA A 646 -31.697 14.321 -13.154 1.00 20.35 O

ANISOU 2638 O ALA A 646 4022 2290 1420 563 -935 -174 O

ATOM 2639 N PRO A 647 -32.604 12.290 -12.752 1.00 19.45 N

ANISOU 2639 N PRO A 647 3911 2141 1339 517 -1024 -218 N

ATOM 2640 CD PRO A 647 -32.537 10.839 -12.492 1.00 18.87 C

ANISOU 2640 CD PRO A 647 3859 2045 1267 500 -1042 -244 C

ATOM 2641 CA PRO A 647 -33.981 12.758 -12.957 1.00 20.45 C

ANISOU 2641 CA PRO A 647 4006 2263 1500 496 -1107 -220 C

ATOM 2642 CB PRO A 647 -34.791 11.457 -12.992 1.00 22.88 C

ANISOU 2642 CB PRO A 647 4328 2540 1824 467 -1185 -253 C

ATOM 2643 CG PRO A 647 -33.970 10.484 -12.175 1.00 22.95 C

ANISOU 2643 CG PRO A 647 4328 2548 1843 454 -1129 -261 C

ATOM 2644 C PRO A 647 -34.488 13.672 -11.839 1.00 26.85 C

ANISOU 2644 C PRO A 647 4704 3103 2393 463 -1087 -199 C

ATOM 2645 O PRO A 647 -35.434 14.421 -12.051 1.00 22.09 O

ANISOU 2645 O PRO A 647 4073 2504 1816 457 -1135 -192 O

ATOM 2646 N ILE A 648 -33.873 13.602 -10.663 1.00 17.57 N

ANISOU 2646 N ILE A 648 3468 1948 1261 444 -1018 -190 N

ATOM 2647 CA ILE A 648 -34.248 14.475 -9.556 1.00 18.13 C ANISOU 2647 CA ILE A 648 3438 2045 1405 414 -990 -169 C

ATOM 2648 CB ILE A 648 -34.994 13.703 -8.447 1.00 17.93 C

ANISOU 2648 CB ILE A 648 3344 2014 1456 364 -1014 -182 C

ATOM 2649 CG2 ILE A 648 -35.337 14.640 -7.292 1.00 15.71 C

ANISOU 2649 CG2 ILE A 648 2963 1758 1247 337 -979 -159 C

ATOM 2650 CGI ILE A 648 -36.252 13.030 -9.008 1.00 22.62 C

ANISOU 2650 CGI ILE A 648 3952 2578 2063 346 -1115 -205 C

ATOM 2651 CD1 ILE A 648 -36.856 11.983 -8.077 1.00 27.70 C

ANISOU 2651 CD 1 ILE A 648 4547 3207 2770 299 -1137 -222 C

ATOM 2652 C ILE A 648 -32.994 15.067 -8.935 1.00 17.19 C

ANISOU 2652 C ILE A 648 3296 1953 1282 428 -891 -148 C

ATOM 2653 O ILE A 648 -32.088 14.333 -8.529 1.00 19.93 O

ANISOU 2653 O ILE A 648 3655 2299 1617 430 -845 -154 O

ATOM 2654 N GLN A 649 -32.941 16.390 -8.854 1.00 18.69 N

ANISOU 2654 N GLN A 649 3453 2165 1482 437 -859 -122 N

ATOM 2655 CA GLN A 649 -31.780 17.055 -8.280 1.00 18.10 C

ANISOU 2655 CA GLN A 649 3355 2115 1408 447 -768 -101 C

ATOM 2656 CB GLN A 649 -30.967 17.723 -9.395 1.00 17.78 C

ANISOU 2656 CB GLN A 649 3383 2076 1296 495 -734 -89 C

ATOM 2657 CG GLN A 649 -30.721 16.753 -10.555 1.00 15.07 C

ANISOU 2657 CG GLN A 649 3139 1704 881 525 -766 -109 C

ATOM 2658 CD GLN A 649 -29.726 17.246 -11.591 1.00 18.82 C

ANISOU 2658 CD GLN A 649 3690 2178 1283 575 -718 -97 C

ATOM 2659 OEl GLN A 649 -28.959 16.454 -12.145 1.00 17.12 O

ANISOU 2659 OEl GLN A 649 3541 1946 1015 601 -699 -108 O

ATOM 2660 NE2 GLN A 649 -29.745 18.549 -11.875 1.00 14.44 N

ANISOU 2660 NE2 GLN A 649 3127 1637 724 590 -696 -74 N

ATOM 2661 C GLN A 649 -32.224 18.033 -7.183 1.00 17.28 C

ANISOU 2661 C GLN A 649 3157 2034 1373 418 -746 -81 C

ATOM 2662 O GLN A 649 -33.120 18.841 -7.385 1.00 19.08 O

ANISOU 2662 O GLN A 649 3363 2265 1622 414 -780 -71 O

ATOM 2663 N ALA A 650 -31.614 17.916 -6.011 1.00 15.60 N

ANISOU 2663 N ALA A 650 2894 1836 1198 398 -690 -76 N

ATOM 2664 CA ALA A 650 -32.054 18.660 -4.837 1.00 9.86 C

ANISOU 2664 CA ALA A 650 2082 1127 539 367 -669 -60 C

ATOM 2665 CB ALA A 650 -32.680 17.696 -3.825 1.00 12.13 C

ANISOU 2665 CB ALA A 650 2325 1404 881 327 -693 -75 C

ATOM 2666 C ALA A 650 -30.902 19.421 -4.193 1.00 16.51 C

ANISOU 2666 C ALA A 650 2898 1992 1382 374 -586 -41 C

ATOM 2667 O ALA A 650 -29.782 18.905 -4.090 1.00 13.48 O

ANISOU 2667 O ALA A 650 2537 1611 974 386 -542 -45 O

ATOM 2668 N MET A 651 -31.183 20.644 -3.754 1.00 10.46 N

ANISOU 2668 N MET A 651 2083 1241 649 365 -565 -19 N

ATOM 2669 CA MET A 651 -30.243 21.412 -2.937 1.00 13.89 C

ANISOU 2669 CA MET A 651 2482 1698 1099 362 -491 -2 C

ATOM 2670 CB MET A 651 -30.579 22.907 -3.018 1.00 11.98 C ANISOU 2670 CB MET A 651 2214 1467 869 366 -476 22 C

ATOM 2671 CG MET A 651 -30.559 23.454 -4.458 1.00 11.34 C

ANISOU 2671 CG MET A 651 2196 1381 732 404 -491 28 C

ATOM 2672 SD MET A 651 -28.877 23.695 -5.051 1.00 18.24 S

ANISOU 2672 SD MET A 651 3120 2263 1548 440 -417 37 S

ATOM 2673 CE MET A 651 -28.269 24.858 -3.828 1.00 13.52 C

ANISOU 2673 CE MET A 651 2451 1689 997 419 -346 60 C

ATOM 2674 C MET A 651 -30.341 20.961 -1.494 1.00 15.30 C

ANISOU 2674 C MET A 651 2600 1880 1334 326 -477 -6 C

ATOM 2675 O MET A 651 -31.444 20.817 -0.967 1.00 11.93 O

ANISOU 2675 O MET A 651 2135 1445 953 299 -514 -9 O

ATOM 2676 N TRP A 652 -29.199 20.747 -0.842 1.00 13.84 N

ANISOU 2676 N TRP A 652 2406 1705 1146 327 -423 -5 N

ATOM 2677 CA TRP A 652 -29.224 20.301 0.551 1.00 9.12 C

ANISOU 2677 CA TRP A 652 1759 1109 597 296 -408 -8 C

ATOM 2678 CB TRP A 652 -29.274 18.769 0.623 1.00 7.73 C

ANISOU 2678 CB TRP A 652 1606 915 414 290 -436 -32 C

ATOM 2679 CG TRP A 652 -29.204 18.198 2.042 1.00 12.07 C

ANISOU 2679 CG TRP A 652 2113 1464 1008 261 -418 -37 C

ATOM 2680 CD2 TRP A 652 -28.201 17.309 2.559 1.00 9.33 C

ANISOU 2680 CD2 TRP A 652 1778 1117 650 266 -390 -46 C

ATOM 2681 CE2 TRP A 652 -28.532 17.033 3.905 1.00 11.73 C

ANISOU 2681 CE2 TRP A 652 2037 1417 1001 236 -382 -47 C

ATOM 2682 CE3 TRP A 652 -27.049 16.725 2.014 1.00 9.88 C

ANISOU 2682 CE3 TRP A 652 1892 1188 673 295 -368 -53 C

ATOM 2683 CDl TRP A 652 -30.088 18.413 3.065 1.00 15.05 C

ANISOU 2683 CDl TRP A 652 2439 1839 1441 229 -425 -32 C

ATOM 2684 NEl TRP A 652 -29.689 17.715 4.195 1.00 12.14 N

ANISOU 2684 NEl TRP A 652 2051 1467 1093 213 -402 -38 N

ATOM 2685 CZ2 TRP A 652 -27.760 16.193 4.707 1.00 10.19 C

ANISOU 2685 CZ2 TRP A 652 1843 1220 807 234 -358 -55 C

ATOM 2686 CZ3 TRP A 652 -26.282 15.894 2.815 1.00 13.56 C

ANISOU 2686 CZ3 TRP A 652 2354 1654 1144 293 -343 -61 C

ATOM 2687 CH2 TRP A 652 -26.641 15.635 4.145 1.00 12.71 C

ANISOU 2687 CH2 TRP A 652 2203 1543 1083 263 -340 -62 C

ATOM 2688 C TRP A 652 -28.053 20.802 1.389 1.00 15.70 C

ANISOU 2688 C TRP A 652 2565 1961 1438 296 -342 4 C

ATOM 2689 0 TRP A 652 -26.893 20.525 1.078 1.00 14.43 O

ANISOU 2689 O TRP A 652 2433 1806 1244 318 -310 2 O

ATOM 2690 N LEU A 653 -28.388 21.567 2.426 1.00 10.00 N

ANISOU 2690 N LEU A 653 1789 1247 762 271 -324 16 N

ATOM 2691 CA LEU A 653 -27.541 21.776 3.604 1.00 10.39 C

ANISOU 2691 CA LEU A 653 1804 1309 834 259 -275 22 C

ATOM 2692 CB LEU A 653 -27.041 20.431 4.176 1.00 10.24 C

ANISOU 2692 CB LEU A 653 1794 1283 815 255 -275 5 C

ATOM 2693 CG LEU A 653 -26.383 20.536 5.558 1.00 13.15 C ANISOU 2693 CG LEU A 653 2124 1660 1213 238 -236 9 C ATOM 2694 CDl LEU A 653 -27.385 21.070 6.601 1.00 10.36 C ANISOU 2694 CDl LEU A 653 1725 1302 909 207 -241 17 C ATOM 2695 CD2 LEU A 653 -25.764 19.210 6.026 1.00 14.03 C ANISOU 2695 CD2 LEU A 653 2250 1764 1317 240 -235 -8 C

ATOM 2696 C LEU A 653 -26.374 22.757 3.432 1.00 13.31 C

ANISOU 2696 C LEU A 653 2174 1697 1185 277 -222 38 C

ATOM 2697 O LEU A 653 -26.166 23.611 4.283 1.00 8.39 O

ANISOU 2697 O LEU A 653 1513 1084 591 262 -191 50 O

ATOM 2698 N GLY A 654 -25.613 22.634 2.352 1.00 9.94 N

ANISOU 2698 N GLY A 654 1792 1272 713 307 -211 36 N ATOM 2699 CA GLY A 654 -24.414 23.443 2.212 1.00 10.84 C ANISOU 2699 CA GLY A 654 1905 1402 814 323 -157 50 C

ATOM 2700 C GLY A 654 -24.657 24.897 1.854 1.00 13.91 C

ANISOU 2700 C GLY A 654 2284 1796 1204 325 -140 70 C

ATOM 2701 O GLY A 654 -23.867 25.765 2.210 1.00 19.50 O

ANISOU 2701 O GLY A 654 2971 2517 1922 324 -93 84 O

ATOM 2702 N TYR A 655 -25.753 25.168 1.147 1.00 8.03 N

ANISOU 2702 N TYR A 655 1556 1042 450 329 -179 72 N ATOM 2703 CA TYR A 655 -25.987 26.489 0.585 1.00 10.84 C ANISOU 2703 CA TYR A 655 1917 1403 800 339 -166 92 C ATOM 2704 CB TYR A 655 -26.066 26.420 -0.942 1.00 9.83 C ANISOU 2704 CB TYR A 655 1851 1266 618 374 -185 91 C ATOM 2705 CG TYR A 655 -26.122 27.785 -1.555 1.00 15.99 C ANISOU 2705 CG TYR A 655 2640 2049 1385 388 -163 112 C ATOM 2706 CDl TYR A 655 -25.001 28.606 -1.551 1.00 13.01 C ANISOU 2706 CDl TYR A 655 2260 1682 1001 397 -100 127 C ATOM 2707 CE1 TYR A 655 -25.049 29.872 -2.094 1.00 14.26 C ANISOU 2707 CE1 TYR A 655 2430 1841 1148 409 -76 147 C ATOM 2708 CD2 TYR A 655 -27.303 28.273 -2.108 1.00 10.37 C ANISOU 2708 CD2 TYR A 655 1939 1330 671 393 -206 117 C ATOM 2709 CE2 TYR A 655 -27.363 29.537 -2.650 1.00 14.49 C ANISOU 2709 CE2 TYR A 655 2473 1854 1180 407 -186 137 C ATOM 2710 CZ TYR A 655 -26.231 30.334 -2.640 1.00 13.18 C ANISOU 2710 CZ TYR A 655 2307 1696 1005 415 -119 152 C ATOM 2711 OH TYR A 655 -26.281 31.601 -3.181 1.00 21.71 O ANISOU 2711 OH TYR A 655 3402 2776 2072 430 -95 173 O

ATOM 2712 C TYR A 655 -27.297 27.068 1.135 1.00 11.10 C

ANISOU 2712 C TYR A 655 1912 1433 873 316 -195 98 C

ATOM 2713 O TYR A 655 -28.363 26.511 0.904 1.00 16.49 O

ANISOU 2713 O TYR A 655 2600 2104 1562 311 -248 89 O

ATOM 2714 N PRO A 656 -27.206 28.185 1.867 1.00 15.99 N ANISOU 2714 N PRO A 656 2493 2061 1521 301 -160 115 N ATOM 2715 CD PRO A 656 -25.960 28.872 2.245 1.00 12.44 C ANISOU 2715 CD PRO A 656 2032 1624 1071 302 -100 125 C ATOM 2716 CA PRO A 656 -28.371 28.748 2.559 1.00 16.59 C ANISOU 2716 CA PRO A 656 2529 2133 1640 278 -179 123 C

ATOM 2717 CB PRO A 656 -27.741 29.398 3.785 1.00 6.73 C

ANISOU 2717 CB PRO A 656 1241 894 423 257 -130 131 C

ATOM 2718 CG PRO A 656 -26.423 29.895 3.265 1.00 17.37 C

ANISOU 2718 CG PRO A 656 2610 2251 1739 276 -84 139 C

ATOM 2719 C PRO A 656 -29.118 29.784 1.716 1.00 18.46 C

ANISOU 2719 C PRO A 656 2780 2368 1868 294 -193 138 C

ATOM 2720 O PRO A 656 -29.270 30.936 2.128 1.00 16.74 O

ANISOU 2720 O PRO A 656 2536 2153 1669 286 -166 156 O

ATOM 2721 N GLY A 657 -29.570 29.371 0.541 1.00 11.18 N

ANISOU 2721 N GLY A 657 1899 1438 912 316 -235 132 N ATOM 2722 CA GLY A 657 -30.398 30.221 -0.310 1.00 11.63 C ANISOU 2722 CA GLY A 657 1972 1490 958 333 -259 145 C

ATOM 2723 C GLY A 657 -30.846 29.456 -1.532 1.00 15.75 C

ANISOU 2723 C GLY A 657 2545 2000 1441 356 -315 132 C

ATOM 2724 O GLY A 657 -30.525 28.269 -1.675 1.00 15.23 O

ANISOU 2724 O GLY A 657 2500 1929 1358 357 -332 113 O

ATOM 2725 N THR A 658 -31.589 30.114 -2.422 1.00 12.91 N

ANISOU 2725 N THR A 658 2206 1634 1064 376 -346 142 N

ATOM 2726 CA THR A 658 -32.018 29.454 -3.642 1.00 19.04 C ANISOU 2726 CA THR A 658 3038 2398 1799 400 -403 129 C

ATOM 2727 CB THR A 658 -33.271 30.125 -4.256 1.00 8.91 C

ANISOU 2727 CB THR A 658 1756 1108 522 412 -455 139 C ATOM 2728 OG1 THR A 658 -33.719 29.369 -5.379 1.00 21.89 O ANISOU 2728 OG1 THR A 658 3454 2737 2127 432 -519 123 O ATOM 2729 CG2 THR A 658 -32.967 31.567 -4.697 1.00 16.06 C ANISOU 2729 CG2 THR A 658 2678 2018 1405 434 -414 164 C

ATOM 2730 C THR A 658 -30.900 29.413 -4.672 1.00 12.45 C

ANISOU 2730 C THR A 658 2271 1562 898 434 -373 129 C

ATOM 2731 O THR A 658 -30.072 30.315 -4.752 1.00 16.63 O

ANISOU 2731 O THR A 658 2808 2099 1412 446 -314 146 O

ATOM 2732 N SER A 659 -30.868 28.346 -5.459 1.00 10.11 N

ANISOU 2732 N SER A 659 2026 1253 563 450 -411 110 N

ATOM 2733 CA SER A 659 -29.954 28.275 -6.584 1.00 17.48 C ANISOU 2733 CA SER A 659 3033 2180 1430 487 -388 111 C

ATOM 2734 CB SER A 659 -29.860 26.837 -7.083 1.00 14.28 C

ANISOU 2734 CB SER A 659 2672 1761 992 495 -426 85 C

ATOM 2735 OG SER A 659 -31.059 26.491 -7.771 1.00 18.00 O

ANISOU 2735 OG SER A 659 3168 2216 1454 501 -508 74 O

ATOM 2736 C SER A 659 -30.479 29.152 -7.718 1.00 19.22 C

ANISOU 2736 C SER A 659 3299 2391 1611 519 -411 124 C

ATOM 2737 O SER A 659 -29.740 29.537 -8.618 1.00 15.79 O

ANISOU 2737 O SER A 659 2923 1952 1124 552 -377 133 O

ATOM 2738 N GLY A 660 -31.772 29.457 -7.679 1.00 17.91 N

ANISOU 2738 N GLY A 660 3108 2222 1475 510 -469 126 N ATOM 2739 CA GLY A 660 -32.389 30.248 -8.728 1.00 18.69 C ANISOU 2739 CA GLY A 660 3249 2312 1540 541 -501 138 C

ATOM 2740 C GLY A 660 -32.388 29.531 -10.065 1.00 24.09 C

ANISOU 2740 C GLY A 660 4020 2976 2156 575 -546 123 C

ATOM 2741 O GLY A 660 -32.805 30.094 -11.079 1.00 25.42 O

ANISOU 2741 O GLY A 660 4240 3134 2285 606 -576 131 O

ATOM 2742 N ALA A 661 -31.957 28.272 -10.063 1.00 18.17 N

ANISOU 2742 N ALA A 661 3291 2221 1393 569 -555 101 N

ATOM 2743 CA ALA A 661 -31.636 27.570 -11.307 1.00 19.29 C

ANISOU 2743 CA ALA A 661 3525 2343 1461 604 -580 87 C

ATOM 2744 CB ALA A 661 -30.268 26.906 -11.187 1.00 25.36 C

ANISOU 2744 CB ALA A 661 4317 3114 2206 610 -515 81 C

ATOM 2745 C ALA A 661 -32.680 26.535 -11.729 1.00 21.79 C

ANISOU 2745 C ALA A 661 3863 2642 1775 599 -676 62 C

ATOM 2746 0 ALA A 661 -33.142 25.738 -10.919 1.00 24.00 O

ANISOU 2746 O ALA A 661 4090 2923 2104 564 -706 47 O

ATOM 2747 N LEU A 662 -33.011 26.523 -13.015 1.00 22.69 N

ANISOU 2747 N LEU A 662 4056 2736 1828 635 -725 58 N

ATOM 2748 CA LEU A 662 -33.999 25.583 -13.541 1.00 25.06 C

ANISOU 2748 CA LEU A 662 4385 3017 2121 632 -823 33 C

ATOM 2749 CB LEU A 662 -34.285 25.877 -15.017 1.00 48.95 C

ANISOU 2749 CB LEU A 662 7505 6021 5072 679 -870 34 C

ATOM 2750 CG LEU A 662 -35.150 27.101 -15.342 1.00 65.25 C

ANISOU 2750 CG LEU A 662 9558 8088 7146 692 -901 54 C

ATOM 2751 CDl LEU A 662 -34.635 28.364 -14.658 1.00 72.41 C

ANISOU 2751 CDl LEU A 662 10413 9018 8082 688 -815 84 C

ATOM 2752 CD2 LEU A 662 -35.239 27.303 -16.849 1.00 66.51 C

ANISOU 2752 CD2 LEU A 662 9826 8224 7220 744 -941 54 C

ATOM 2753 C LEU A 662 -33.584 24.115 -13.372 1.00 24.59 C

ANISOU 2753 C LEU A 662 4342 2946 2053 619 -831 6 C

ATOM 2754 0 LEU A 662 -34.439 23.241 -13.230 1.00 25.89 O

ANISOU 2754 O LEU A 662 4492 3101 2246 595 -903 -15 O

ATOM 2755 N PHE A 663 -32.282 23.840 -13.382 1.00 23.45 N

ANISOU 2755 N PHE A 663 4231 2805 1874 633 -757 8 N

ATOM 2756 CA PHE A 663 -31.819 22.450 -13.271 1.00 20.64 C

ANISOU 2756 CA PHE A 663 3899 2438 1507 625 -760 -16 C

ATOM 2757 CB PHE A 663 -30.409 22.268 -13.845 1.00 21.80 C

ANISOU 2757 CB PHE A 663 4114 2579 1589 661 -687 -12 C

ATOM 2758 CG PHE A 663 -29.396 23.260 -13.337 1.00 20.97 C

ANISOU 2758 CG PHE A 663 3973 2497 1499 665 -590 14 C

ATOM 2759 CDl PHE A 663 -28.739 23.046 -12.141 1.00 18.37 C

ANISOU 2759 CDl PHE A 663 3573 2187 1219 636 -536 16 C

ATOM 2760 CD2 PHE A 663 -29.076 24.392 -14.081 1.00 22.65 C

ANISOU 2760 CD2 PHE A 663 4225 2709 1672 699 -554 37 C

ATOM 2761 CE1 PHE A 663 -27.785 23.949 -11.679 1.00 23.39 C

ANISOU 2761 CE1 PHE A 663 4176 2843 1870 638 -450 39 C

ATOM 2762 CE2 PHE A 663 -28.122 25.299 -13.625 1.00 16.61 C ANISOU 2762 CE2 PHE A 663 3426 1963 923 700 -464 61 C

ATOM 2763 CZ PHE A 663 -27.479 25.077 -12.425 1.00 15.38 C

ANISOU 2763 CZ PHE A 663 3198 1827 820 669 -414 61 C

ATOM 2764 C PHE A 663 -31.901 21.870 -11.861 1.00 24.43 C

ANISOU 2764 C PHE A 663 4290 2932 2061 577 -749 -24 C

ATOM 2765 O PHE A 663 -31.705 20.664 -11.667 1.00 22.01 O

ANISOU 2765 O PHE A 663 3995 2615 1752 566 -761 -45 O

ATOM 2766 N MET A 664 -32.182 22.711 -10.871 1.00 17.79 N

ANISOU 2766 N MET A 664 3364 2112 1282 551 -724 -7 N

ATOM 2767 CA MET A 664 -32.432 22.185 -9.531 1.00 18.88 C ANISOU 2767 CA MET A 664 3421 2261 1492 506 -720 -14 C

ATOM 2768 CB MET A 664 -31.780 23.042 -8.455 1.00 13.22 C

ANISOU 2768 CB MET A 664 2638 1569 815 490 -641 8 C

ATOM 2769 CG MET A 664 -30.253 23.186 -8.587 1.00 12.93 C

ANISOU 2769 CG MET A 664 2633 1540 739 514 -558 17 C

ATOM 2770 SD MET A 664 -29.309 21.638 -8.655 1.00 16.33 S

ANISOU 2770 SD MET A 664 3107 1959 1137 521 -544 -7 S

ATOM 2771 CE MET A 664 -29.847 20.751 -7.184 1.00 10.13 C

ANISOU 2771 CE MET A 664 2244 1179 427 470 -566 -22 C

ATOM 2772 C MET A 664 -33.932 22.031 -9.269 1.00 25.37 C

ANISOU 2772 C MET A 664 4198 3076 2367 477 -801 -23 C

ATOM 2773 O MET A 664 -34.699 22.975 -9.434 1.00 20.87 O

ANISOU 2773 O MET A 664 3605 2509 1814 479 -825 -8 O

ATOM 2774 N ASP A 665 -34.345 20.839 -8.845 1.00 16.84 N

ANISOU 2774 N ASP A 665 3102 1983 1314 449 -839 -45 N

ATOM 2775 CA ASP A 665 -35.767 20.545 -8.688 1.00 19.16 C

ANISOU 2775 CA ASP A 665 3356 2266 1659 421 -919 -56 C

ATOM 2776 CB ASP A 665 -36.021 19.061 -8.939 1.00 18.79 C

ANISOU 2776 CB ASP A 665 3343 2194 1601 409 -974 -87 C

ATOM 2777 CG ASP A 665 -35.626 18.649 -10.338 1.00 24.65 C

ANISOU 2777 CG ASP A 665 4190 2917 2258 449 -1003 -100 C

ATOM 2778 OD1 ASP A 665 -36.177 19.230 -11.294 1.00 21.08 O ANISOU 2778 ODl ASP A 665 3774 2458 1777 472 -1050 -96 O

ATOM 2779 OD2 ASP A 665 -34.755 17.773 -10.482 1.00 19.74 O ANISOU 2779 OD2 ASP A 665 3617 2287 1597 459 -976 -113 O

ATOM 2780 C ASP A 665 -36.308 20.945 -7.323 1.00 25.97 C

ANISOU 2780 C ASP A 665 4119 3144 2606 382 -898 -44 C

ATOM 2781 O ASP A 665 -37.395 21.530 -7.223 1.00 18.44 O

ANISOU 2781 O ASP A 665 3119 2190 1696 370 -938 -36 O

ATOM 2782 N TYR A 666 -35.531 20.643 -6.284 1.00 17.06 N

ANISOU 2782 N TYR A 666 2957 2026 1498 364 -835 -42 N

ATOM 2783 CA TYR A 666 -35.975 20.793 -4.903 1.00 17.94 C

ANISOU 2783 CA TYR A 666 2983 2147 1687 325 -813 -35 C

ATOM 2784 CB TYR A 666 -36.229 19.420 -4.278 1.00 11.86 C

ANISOU 2784 CB TYR A 666 2198 1362 948 294 -835 -57 C

ATOM 2785 CG TYR A 666 -37.414 18.671 -4.832 1.00 19.49 C ANISOU 2785 CG TYR A 666 3171 2303 1929 281 -923 -77 C ATOM 2786 CDl TYR A 666 -38.713 19.045 -4.503 1.00 23.02 C ANISOU 2786 CDl TYR A 666 3556 2747 2442 257 -966 -71 C ATOM 2787 CEl TYR A 666 -39.807 18.350 -5.003 1.00 17.48 C ANISOU 2787 CEl TYR A 666 2856 2023 1761 243 -1050 -90 C ATOM 2788 CD2 TYR A 666 -37.237 17.569 -5.662 1.00 19.74 C ANISOU 2788 CD2 TYR A 666 3271 2314 1914 292 -965 -102 C ATOM 2789 CE2 TYR A 666 -38.329 16.867 -6.164 1.00 21.63 C ANISOU 2789 CE2 TYR A 666 3518 2530 2170 277 -1051 -122 C ATOM 2790 CZ TYR A 666 -39.609 17.264 -5.829 1.00 21.43 C ANISOU 2790 CZ TYR A 666 3427 2503 2214 252 -1094 -116 C ATOM 2791 OH TYR A 666 -40.694 16.569 -6.324 1.00 21.58 O ANISOU 2791 OH TYR A 666 3447 2497 2254 235 -1182 -135 O ATOM 2792 C TYR A 666 -34.939 21.491 -4.038 1.00 14.08 C ANISOU 2792 C TYR A 666 2465 1680 1204 325 -725 -16 C ATOM 2793 O TYR A 666 -33.755 21.433 -4.319 1.00 15.19 O ANISOU 2793 O TYR A 666 2648 1827 1297 347 -679 -15 O ATOM 2794 N ILE A 667 -35.404 22.152 -2.986 1.00 12.78 N ANISOU 2794 N ILE A 667 2229 1526 1100 300 -702 -1 N ATOM 2795 CA ILE A 667 -34.525 22.546 -1.900 1.00 14.26 C ANISOU 2795 CA ILE A 667 2383 1731 1306 290 -627 11 C ATOM 2796 CB ILE A 667 -34.418 24.080 -1.743 1.00 12.55 C ANISOU 2796 CB ILE A 667 2141 1531 1097 298 -586 38 C ATOM 2797 CG2 ILE A 667 -35.793 24.713 -1.533 1.00 13.49 C ANISOU 2797 CG2 ILE A 667 2211 1646 1267 284 -623 49 C ATOM 2798 CGI ILE A 667 -33.462 24.419 -0.592 1.00 13.57 C ANISOU 2798 CGI ILE A 667 2238 1676 1244 286 -512 48 C ATOM 2799 CDl ILE A 667 -33.098 25.903 -0.507 1.00 17.64 C ANISOU 2799 CDl ILE A 667 2739 2207 1758 296 -464 74 C ATOM 2800 C ILE A 667 -35.013 21.859 -0.626 1.00 17.29 C ANISOU 2800 C ILE A 667 2711 2108 1751 250 -627 4 C ATOM 2801 O ILE A 667 -36.201 21.901 -0.287 1.00 15.41 O ANISOU 2801 O ILE A 667 2430 1862 1565 228 -662 5 O ATOM 2802 N ILE A 668 -34.095 21.193 0.062 1.00 11.59 N ANISOU 2802 N ILE A 668 1991 1388 1023 243 -586 -4 N ATOM 2803 CA ILE A 668 -34.441 20.476 1.265 1.00 10.27 C ANISOU 2803 CA ILE A 668 1781 1213 907 210 -581 -11 C ATOM 2804 CB ILE A 668 -33.532 19.231 1.468 1.00 13.71 C ANISOU 2804 CB ILE A 668 2250 1643 1317 211 -566 -30 C ATOM 2805 CG2 ILE A 668 -33.801 18.570 2.814 1.00 16.28 C ANISOU 2805 CG2 ILE A 668 2533 1960 1694 178 -552 -35 C ATOM 2806 CGI ILE A 668 -33.783 18.222 0.336 1.00 12.28 C ANISOU 2806 CGI ILE A 668 2124 1443 1099 223 -623 -51 C ATOM 2807 CDl ILE A 668 -32.927 16.953 0.418 1.00 14.96 C ANISOU 2807 CDl ILE A 668 2502 1772 1408 228 -611 -70 C ATOM 2808 C ILE A 668 -34.387 21.459 2.421 1.00 13.84 C ANISOU 2808 C ILE A 668 2178 1679 1401 194 -529 10 C

ATOM 2809 O ILE A 668 -33.345 22.034 2.727 1.00 14.32 O

ANISOU 2809 O ILE A 668 2242 1756 1442 205 -476 20 O

ATOM 2810 N THR A 669 -35.535 21.674 3.044 1.00 12.65 N

ANISOU 2810 N THR A 669 1977 1520 1308 169 -546 16 N

ATOM 2811 CA THR A 669 -35.657 22.724 4.038 1.00 10.96 C

ANISOU 2811 CA THR A 669 1715 1317 1133 157 -502 37 C

ATOM 2812 CB THR A 669 -35.952 24.096 3.363 1.00 14.22 C

ANISOU 2812 CB THR A 669 2126 1741 1538 176 -503 56 C

ATOM 2813 OG1 THR A 669 -36.013 25.137 4.339 1.00 10.82 O

ANISOU 2813 OG1 THR A 669 1652 1318 1141 165 -457 77 O

ATOM 2814 CG2 THR A 669 -37.252 24.067 2.544 1.00 14.72 C

ANISOU 2814 CG2 THR A 669 2183 1792 1618 178 -571 54 C

ATOM 2815 C THR A 669 -36.711 22.270 5.031 1.00 10.39 C

ANISOU 2815 C THR A 669 1594 1228 1126 124 -513 35 C

ATOM 2816 O THR A 669 -36.895 21.072 5.223 1.00 13.48 O

ANISOU 2816 O THR A 669 1991 1603 1527 109 -534 17 O

ATOM 2817 N ASP A 670 -37.381 23.202 5.691 1.00 15.22 N

ANISOU 2817 N ASP A 670 2159 1841 1783 112 -494 54 N

ATOM 2818 CA ASP A 670 -38.470 22.831 6.592 1.00 17.05 C

ANISOU 2818 CA ASP A 670 2343 2055 2081 82 -501 55 C

ATOM 2819 CB ASP A 670 -37.941 22.394 7.965 1.00 10.92 C

ANISOU 2819 CB ASP A 670 1554 1273 1320 63 -450 53 C

ATOM 2820 CG ASP A 670 -37.155 23.483 8.658 1.00 17.66 C

ANISOU 2820 CG ASP A 670 2402 2143 2164 69 -391 70 C

ATOM 2821 OD1 ASP A 670 -37.763 24.303 9.384 1.00 14.79 O

ANISOU 2821 OD1 ASP A 670 2001 1777 1842 59 -366 88 O

ATOM 2822 OD2 ASP A 670 -35.923 23.515 8.480 1.00 13.11 O

ANISOU 2822 OD2 ASP A 670 1859 1582 1540 85 -368 67 O

ATOM 2823 C ASP A 670 -39.416 24.010 6.742 1.00 16.33 C

ANISOU 2823 C ASP A 670 2207 1965 2032 80 -498 77 C

ATOM 2824 O ASP A 670 -39.119 25.114 6.270 1.00 9.37 O

ANISOU 2824 O ASP A 670 1335 1099 1125 101 -485 91 O

ATOM 2825 N GLN A 671 -40.543 23.771 7.406 1.00 14.54 N

ANISOU 2825 N GLN A 671 1933 1720 1869 56 -507 80 N

ATOM 2826 CA GLN A 671 -41.619 24.756 7.489 1.00 18.66 C

ANISOU 2826 CA GLN A 671 2409 2240 2439 54 -511 101 C

ATOM 2827 CB GLN A 671 -42.891 24.115 8.068 1.00 17.05 C

ANISOU 2827 CB GLN A 671 2156 2013 2310 26 -531 99 C

ATOM 2828 CG GLN A 671 -44.072 25.070 8.158 1.00 31.61 C

ANISOU 2828 CG GLN A 671 3946 3852 4210 25 -536 121 C

ATOM 2829 CD GLN A 671 -45.232 24.490 8.950 1.00 52.98 C

ANISOU 2829 CD GLN A 671 6598 6533 6997 -5 -538 122 C

ATOM 2830 OEl GLN A 671 -45.351 23.273 9.100 1.00 46.88 O

ANISOU 2830 OEl GLN A 671 5829 5745 6237 -25 -557 103 O

ATOM 2831 NE2 GLN A 671 -46.093 25.363 9.463 1.00 63.75 N ANISOU 2831 NE2 GLN A 671 7913 7893 8416 -8 -516 145 N

ATOM 2832 C GLN A 671 -41.228 25.984 8.308 1.00 14.85 C

ANISOU 2832 C GLN A 671 1912 1769 1960 59 -447 123 C

ATOM 2833 0 GLN A 671 -41.742 27.074 8.076 1.00 12.26 O

ANISOU 2833 O GLN A 671 1564 1446 1647 70 -445 142 O

ATOM 2834 N GLU A 672 -40.332 25.817 9.276 1.00 10.92 N

ANISOU 2834 N GLU A 672 1426 1273 1450 50 -395 121 N

ATOM 2835 CA GLU A 672 -39.843 26.980 10.046 1.00 11.81 C

ANISOU 2835 CA GLU A 672 1531 1395 1559 54 -336 140 C

ATOM 2836 CB GLU A 672 -39.180 26.539 11.363 1.00 18.73 C

ANISOU 2836 CB GLU A 672 2412 2265 2439 36 -287 136 C

ATOM 2837 CG GLU A 672 -40.094 25.779 12.318 1.00 16.24 C

ANISOU 2837 CG GLU A 672 2065 1924 2181 10 -283 134 C

ATOM 2838 CD GLU A 672 -41.320 26.583 12.738 1.00 21.21 C

ANISOU 2838 CD GLU A 672 2646 2542 2869 3 -271 155 C

ATOM 2839 OE1 GLU A 672 -41.180 27.789 13.031 1.00 15.46 O

ANISOU 2839 OE1 GLU A 672 1913 1821 2139 12 -236 173 O

ATOM 2840 OE2 GLU A 672 -42.422 25.996 12.797 1.00 20.96 O

ANISOU 2840 OE2 GLU A 672 2583 2492 2890 -12 -296 153 O

ATOM 2841 C GLU A 672 -38.857 27.835 9.238 1.00 14.42 C

ANISOU 2841 C GLU A 672 1898 1749 1833 80 -326 145 C

ATOM 2842 0 GLU A 672 -38.912 29.071 9.254 1.00 13.92 O

ANISOU 2842 O GLU A 672 1826 1693 1772 90 -302 165 O

ATOM 2843 N THR A 673 -37.947 27.171 8.533 1.00 13.19 N

ANISOU 2843 N THR A 673 1784 1602 1626 92 -342 129 N

ATOM 2844 CA THR A 673 -36.948 27.876 7.732 1.00 11.70 C

ANISOU 2844 CA THR A 673 1631 1432 1383 118 -330 133 C

ATOM 2845 CB THR A 673 -35.855 26.904 7.246 1.00 4.64 C

ANISOU 2845 CB THR A 673 780 543 438 127 -337 113 C

ATOM 2846 OG1 THR A 673 -35.259 26.278 8.391 1.00 10.48 O

ANISOU 2846 OG1 THR A 673 1515 1280 1189 109 -304 105 O

ATOM 2847 CG2 THR A 673 -34.789 27.640 6.427 1.00 6.17 C

ANISOU 2847 CG2 THR A 673 1011 755 579 154 -317 119 C

ATOM 2848 C THR A 673 -37.609 28.541 6.539 1.00 13.54 C

ANISOU 2848 C THR A 673 1869 1668 1606 139 -367 142 C

ATOM 2849 0 THR A 673 -37.319 29.688 6.204 1.00 16.69 O

ANISOU 2849 O THR A 673 2277 2078 1987 155 -345 158 O

ATOM 2850 N SER A 674 -38.511 27.811 5.899 1.00 12.07 N

ANISOU 2850 N SER A 674 1681 1472 1435 137 -426 131 N

ATOM 2851 CA SER A 674 -39.044 28.238 4.616 1.00 10.08 C

ANISOU 2851 CA SER A 674 1445 1221 1164 161 -473 135 C

ATOM 2852 CB SER A 674 -38.352 27.455 3.499 1.00 13.38 C

ANISOU 2852 CB SER A 674 1920 1642 1522 179 -505 116 C

ATOM 2853 OG SER A 674 -36.944 27.533 3.656 1.00 14.35 O

ANISOU 2853 OG SER A 674 2074 1777 1601 188 -455 115 O

ATOM 2854 C SER A 674 -40.549 28.026 4.553 1.00 15.03 C ANISOU 2854 C SER A 674 2031 1834 1848 149 -524 136 C

ATOM 2855 O SER A 674 -41.026 27.122 3.867 1.00 14.93 O

ANISOU 2855 O SER A 674 2029 1811 1833 148 -582 120 O

ATOM 2856 N PRO A 675 -41.307 28.857 5.282 1.00 17.50 N

ANISOU 2856 N PRO A 675 2295 2143 2212 140 -501 156 N

ATOM 2857 CD PRO A 675 -40.836 29.950 6.148 1.00 17.33 C

ANISOU 2857 CD PRO A 675 2260 2129 2194 139 -433 176 C

ATOM 2858 CA PRO A 675 -42.771 28.735 5.285 1.00 17.24 C

ANISOU 2858 CA PRO A 675 2214 2096 2242 129 -544 160 C

ATOM 2859 CB PRO A 675 -43.233 29.952 6.108 1.00 18.49 C

ANISOU 2859 CB PRO A 675 2329 2254 2441 127 -497 187 C

ATOM 2860 CG PRO A 675 -42.035 30.838 6.240 1.00 20.14 C

ANISOU 2860 CG PRO A 675 2572 2479 2600 142 -441 197 C

ATOM 2861 C PRO A 675 -43.340 28.784 3.873 1.00 21.76 C

ANISOU 2861 C PRO A 675 2804 2668 2796 151 -616 157 C

ATOM 2862 O PRO A 675 -42.791 29.458 3.004 1.00 19.06 O

ANISOU 2862 O PRO A 675 2503 2338 2399 180 -618 162 O

ATOM 2863 N ALA A 676 -44.429 28.062 3.646 1.00 20.11 N

ANISOU 2863 N ALA A 676 2565 2444 2631 138 -675 147 N

ATOM 2864 CA ALA A 676 -44.990 27.945 2.305 1.00 31.47 C

ANISOU 2864 CA ALA A 676 4024 3880 4052 158 -753 139 C

ATOM 2865 CB ALA A 676 -46.202 27.030 2.314 1.00 42.42 C

ANISOU 2865 CB ALA A 676 5369 5248 5502 134 -814 127 C

ATOM 2866 C ALA A 676 -45.346 29.313 1.736 1.00 35.24 C

ANISOU 2866 C ALA A 676 4500 4368 4523 187 -758 163 C

ATOM 2867 O ALA A 676 -45.371 29.498 0.519 1.00 34.20 O

ANISOU 2867 O ALA A 676 4408 4239 4348 215 -808 159 O

ATOM 2868 N GLU A 677 -45.606 30.270 2.623 1.00 32.20 N

ANISOU 2868 N GLU A 677 4071 3985 4177 183 -705 186 N

ATOM 2869 CA GLU A 677 -45.936 31.632 2.213 1.00 38.71 C

ANISOU 2869 CA GLU A 677 4891 4818 4999 211 -701 211 C

ATOM 2870 CB GLU A 677 -46.223 32.518 3.427 1.00 43.81 C

ANISOU 2870 CB GLU A 677 5487 5462 5695 199 -635 235 C

ATOM 2871 CG GLU A 677 -47.295 31.982 4.360 1.00 52.73 C

ANISOU 2871 CG GLU A 677 6548 6576 6911 169 -637 236 C

ATOM 2872 CD GLU A 677 -46.730 31.070 5.433 1.00 53.50 C

ANISOU 2872 CD GLU A 677 6644 6667 7018 137 -594 222 C

ATOM 2873 OEl GLU A 677 -46.181 31.596 6.426 1.00 54.58 O

ANISOU 2873 OEl GLU A 677 6778 6806 7154 130 -522 234 O

ATOM 2874 OE2 GLU A 677 -46.841 29.831 5.288 1.00 42.25 O

ANISOU 2874 OE2 GLU A 677 5221 5233 5599 120 -632 200 O

ATOM 2875 C GLU A 677 -44.826 32.261 1.386 1.00 38.74 C

ANISOU 2875 C GLU A 677 4964 4836 4920 242 -683 213 C

ATOM 2876 O GLU A 677 -45.087 33.085 0.510 1.00 46.93 O

ANISOU 2876 O GLU A 677 6020 5878 5935 272 -708 226 O

ATOM 2877 N VAL A 678 -43.585 31.880 1.664 1.00 35.54 N ANISOU 2877 N VAL A 678 4596 4437 4469 236 -639 203 N

ATOM 2878 CA VAL A 678 -42.444 32.484 0.978 1.00 29.42 C ANISOU 2878 CA VAL A 678 3883 3676 3621 263 -611 206 C

ATOM 2879 CB VAL A 678 -41.331 32.885 1.960 1.00 32.79 C

ANISOU 2879 CB VAL A 678 4312 4112 4037 252 -527 213 C

ATOM 2880 CGI VAL A 678 -41.860 33.888 2.978 1.00 42.68 C ANISOU 2880 CGI VAL A 678 5512 5362 5340 241 -483 236 C

ATOM 2881 CG2 VAL A 678 -40.755 31.651 2.651 1.00 30.64 C ANISOU 2881 CG2 VAL A 678 4039 3836 3767 225 -514 192 C

ATOM 2882 C VAL A 678 -41.845 31.590 -0.104 1.00 23.37 C

ANISOU 2882 C VAL A 678 3178 2908 2792 278 -651 184 C

ATOM 2883 O VAL A 678 -40.702 31.785 -0.500 1.00 27.62 O

ANISOU 2883 O VAL A 678 3768 3456 3271 295 -617 183 O

ATOM 2884 N ALA A 679 -42.613 30.624 -0.591 1.00 23.73 N

ANISOU 2884 N ALA A 679 3220 2942 2853 272 -723 166 N

ATOM 2885 CA ALA A 679 -42.132 29.772 -1.675 1.00 35.86 C ANISOU 2885 CA ALA A 679 4822 4475 4330 288 -766 145 C

ATOM 2886 CB ALA A 679 -43.236 28.827 -2.149 1.00 31.70 C

ANISOU 2886 CB ALA A 679 4281 3932 3832 278 -853 127 C

ATOM 2887 C ALA A 679 -41.586 30.601 -2.844 1.00 32.01 C

ANISOU 2887 C ALA A 679 4398 3994 3772 329 -766 154 C

ATOM 2888 O ALA A 679 -40.725 30.140 -3.591 1.00 27.95 O

ANISOU 2888 O ALA A 679 3947 3479 3193 347 -767 142 O

ATOM 2889 N GLU A 680 -42.091 31.825 -2.985 1.00 25.23 N

ANISOU 2889 N GLU A 680 3522 3139 2925 347 -761 178 N

ATOM 2890 CA GLU A 680 -41.700 32.735 -4.061 1.00 30.93 C ANISOU 2890 CA GLU A 680 4303 3865 3585 388 -759 191 C

ATOM 2891 CB GLU A 680 -42.576 33.992 -4.016 1.00 40.80 C

ANISOU 2891 CB GLU A 680 5517 5116 4869 401 -762 217 C

ATOM 2892 CG GLU A 680 -42.215 35.062 -5.031 1.00 71.37 C ANISOU 2892 CG GLU A 680 9448 8991 8680 443 -753 234 C

ATOM 2893 CD GLU A 680 -43.005 36.344 -4.823 1.00 88.48 C ANISOU 2893 CD GLU A 680 11577 11159 10883 455 -745 261 C

ATOM 2894 OEl GLU A 680 -43.562 36.527 -3.719 1.00 91.25 O ANISOU 2894 OEl GLU A 680 11857 11511 11303 428 -723 270 O

ATOM 2895 OE2 GLU A 680 -43.069 37.169 -5.760 1.00 89.88 O ANISOU 2895 OE2 GLU A 680 11797 11333 11019 492 -759 275 O

ATOM 2896 C GLU A 680 -40.221 33.138 -4.031 1.00 27.83 C

ANISOU 2896 C GLU A 680 3953 3482 3137 398 -682 196 C

ATOM 2897 O GLU A 680 -39.663 33.557 -5.049 1.00 22.67 O

ANISOU 2897 O GLU A 680 3364 2829 2420 432 -678 201 O

ATOM 2898 N GLN A 681 -39.592 33.021 -2.869 1.00 22.01 N

ANISOU 2898 N GLN A 681 3184 2753 2427 370 -620 196 N

ATOM 2899 CA GLN A 681 -38.181 33.371 -2.733 1.00 25.32 C ANISOU 2899 CA GLN A 681 3635 3182 2804 376 -547 201 C

ATOM 2900 CB GLN A 681 -37.801 33.480 -1.255 1.00 26.94 C ANISOU 2900 CB GLN A 681 3787 3394 3054 343 -486 205 C

ATOM 2901 CG GLN A 681 -38.599 34.504 -0.472 1.00 40.41 C

ANISOU 2901 CG GLN A 681 5439 5101 4815 332 -467 227 C

ATOM 2902 CD GLN A 681 -38.304 34.467 1.020 1.00 46.37 C

ANISOU 2902 CD GLN A 681 6146 5858 5613 298 -414 228 C

ATOM 2903 OEl GLN A 681 -38.892 35.223 1.794 1.00 46.66 O

ANISOU 2903 OEl GLN A 681 6141 5894 5696 288 -392 245 O

ATOM 2904 NE2 GLN A 681 -37.394 33.582 1.431 1.00 32.37 N

ANISOU 2904 NE2 GLN A 681 4384 4089 3826 283 -393 211 N

ATOM 2905 C GLN A 681 -37.265 32.353 -3.415 1.00 18.70 C

ANISOU 2905 C GLN A 681 2854 2341 1909 387 -554 180 C

ATOM 2906 O GLN A 681 -36.093 32.635 -3.653 1.00 19.08 O

ANISOU 2906 O GLN A 681 2941 2396 1913 400 -502 184 O

ATOM 2907 N TYR A 682 -37.808 31.174 -3.709 1.00 13.76 N

ANISOU 2907 N TYR A 682 2235 1706 1288 379 -617 158 N

ATOM 2908 CA TYR A 682 -37.026 30.054 -4.234 1.00 17.13 C

ANISOU 2908 CA TYR A 682 2713 2127 1667 386 -626 136 C

ATOM 2909 CB TYR A 682 -37.210 28.824 -3.343 1.00 18.10 C

ANISOU 2909 CB TYR A 682 2799 2246 1831 350 -639 116 C

ATOM 2910 CG TYR A 682 -36.930 29.071 -1.888 1.00 18.42 C

ANISOU 2910 CG TYR A 682 2781 2296 1922 320 -579 124 C

ATOM 2911 CD1 TYR A 682 -37.920 29.548 -1.044 1.00 20.39 C

ANISOU 2911 CD1 TYR A 682 2965 2545 2236 298 -582 136 C

ATOM 2912 CE1 TYR A 682 -37.663 29.784 0.297 1.00 23.35 C

ANISOU 2912 CE1 TYR A 682 3294 2926 2653 272 -527 144 C

ATOM 2913 CD2 TYR A 682 -35.671 28.830 -1.356 1.00 13.49 C

ANISOU 2913 CD2 TYR A 682 2166 1681 1279 314 -519 121 C

ATOM 2914 CE2 TYR A 682 -35.408 29.056 -0.017 1.00 19.31 C

ANISOU 2914 CE2 TYR A 682 2854 2425 2059 288 -469 128 C

ATOM 2915 CZ TYR A 682 -36.405 29.539 0.802 1.00 18.12 C

ANISOU 2915 CZ TYR A 682 2645 2272 1968 267 -473 139 C

ATOM 2916 OH TYR A 682 -36.145 29.764 2.135 1.00 21.51 O

ANISOU 2916 OH TYR A 682 3032 2705 2435 242 -422 146 O

ATOM 2917 C TYR A 682 -37.466 29.676 -5.633 1.00 22.54 C

ANISOU 2917 C TYR A 682 3459 2799 2305 415 -696 125 C

ATOM 2918 O TYR A 682 -38.644 29.750 -5.950 1.00 20.07 O

ANISOU 2918 O TYR A 682 3130 2479 2017 416 -760 125 O

ATOM 2919 N SER A 683 -36.523 29.246 -6.463 1.00 16.39 N

ANISOU 2919 N SER A 683 2751 2017 1459 439 -685 115 N

ATOM 2920 CA SER A 683 -36.867 28.709 -7.767 1.00 17.36 C

ANISOU 2920 CA SER A 683 2941 2123 1531 466 -753 101 C

ATOM 2921 CB SER A 683 -35.699 28.856 -8.740 1.00 23.53 C

ANISOU 2921 CB SER A 683 3807 2903 2232 504 -714 104 C

ATOM 2922 OG SER A 683 -34.539 28.216 -8.226 1.00 27.30 O

ANISOU 2922 OG SER A 683 4287 3386 2701 494 -656 95 O

ATOM 2923 C SER A 683 -37.258 27.245 -7.623 1.00 20.68 C ANISOU 2923 C SER A 683 3356 2531 1968 444 -806 73 C

ATOM 2924 O SER A 683 -38.067 26.730 -8.398 1.00 16.63 O

ANISOU 2924 O SER A 683 2870 2002 1445 451 -885 59 O

ATOM 2925 N GLU A 684 -36.674 26.577 -6.628 1.00 13.22 N

ANISOU 2925 N GLU A 684 2380 1592 1050 416 -764 64 N

ATOM 2926 CA GLU A 684 -36.948 25.162 -6.369 1.00 17.18 C

ANISOU 2926 CA GLU A 684 2876 2081 1569 392 -804 38 C

ATOM 2927 CB GLU A 684 -35.868 24.549 -5.455 1.00 14.05 C

ANISOU 2927 CB GLU A 684 2467 1693 1178 374 -740 32 C

ATOM 2928 CG GLU A 684 -34.421 24.770 -5.911 1.00 13.12 C

ANISOU 2928 CG GLU A 684 2405 1583 997 404 -677 38 C

ATOM 2929 CD GLU A 684 -33.835 26.083 -5.426 1.00 22.96 C

ANISOU 2929 CD GLU A 684 3622 2848 2253 408 -606 64 C

ATOM 2930 OEl GLU A 684 -34.599 26.935 -4.909 1.00 20.97 O

ANISOU 2930 OEl GLU A 684 3318 2603 2048 394 -609 79 O

ATOM 2931 OE2 GLU A 684 -32.604 26.270 -5.568 1.00 22.55 O

ANISOU 2931 OE2 GLU A 684 3599 2803 2164 425 -546 70 O

ATOM 2932 C GLU A 684 -38.302 24.961 -5.695 1.00 22.48 C

ANISOU 2932 C GLU A 684 3476 2746 2317 358 -854 35 C

ATOM 2933 O GLU A 684 -38.835 25.870 -5.051 1.00 18.65 O

ANISOU 2933 O GLU A 684 2933 2272 1882 346 -837 54 O

ATOM 2934 N LYS A 685 -38.853 23.759 -5.837 1.00 15.39 N

ANISOU 2934 N LYS A 685 2585 1832 1432 341 -914 11 N

ATOM 2935 CA LYS A 685 -39.992 23.362 -5.019 1.00 19.04 C

ANISOU 2935 CA LYS A 685 2974 2286 1974 303 -949 6 C

ATOM 2936 CB LYS A 685 -40.670 22.120 -5.593 1.00 16.51 C

ANISOU 2936 CB LYS A 685 2677 1942 1654 292 -1031 -22 C

ATOM 2937 CG LYS A 685 -41.305 22.357 -6.970 1.00 16.26 C

ANISOU 2937 CG LYS A 685 2694 1900 1586 321 -1110 -27 C

ATOM 2938 CD LYS A 685 -42.385 23.441 -6.930 1.00 24.11 C

ANISOU 2938 CD LYS A 685 3632 2899 2628 321 -1138 -6 C

ATOM 2939 CE LYS A 685 -42.955 23.672 -8.336 1.00 28.08 C

ANISOU 2939 CE LYS A 685 4189 3390 3089 354 -1219 -11 C

ATOM 2940 NZ LYS A 685 -44.008 24.722 -8.372 1.00 31.53 N

ANISOU 2940 NZ LYS A 685 4576 3833 3572 359 -1251 10 N

ATOM 2941 C LYS A 685 -39.464 23.079 -3.628 1.00 21.03 C

ANISOU 2941 C LYS A 685 3179 2547 2265 273 -882 8 C

ATOM 2942 O LYS A 685 -38.328 22.621 -3.475 1.00 15.41 O

ANISOU 2942 O LYS A 685 2501 1840 1516 278 -836 2 O

ATOM 2943 N LEU A 686 -40.269 23.374 -2.612 1.00 14.30 N

ANISOU 2943 N LEU A 686 2250 1696 1487 244 -874 19 N

ATOM 2944 CA LEU A 686 -39.858 23.123 -1.240 1.00 14.60 C

ANISOU 2944 CA LEU A 686 2245 1738 1563 216 -813 21 C

ATOM 2945 CB LEU A 686 -40.651 23.989 -0.258 1.00 14.56 C

ANISOU 2945 CB LEU A 686 2165 1739 1629 196 -789 43 C

ATOM 2946 CG LEU A 686 -40.680 25.489 -0.554 1.00 18.26 C ANISOU 2946 CG LEU A 686 2628 2222 2087 220 -768 69 C

ATOM 2947 CDl LEU A 686 -41.651 26.197 0.389 1.00 22.62 C

ANISOU 2947 CDl LEU A 686 3105 2774 2714 200 -754 88 C

ATOM 2948 CD2 LEU A 686 -39.271 26.091 -0.481 1.00 19.66 C

ANISOU 2948 CD2 LEU A 686 2841 2417 2212 239 -698 78 C

ATOM 2949 C LEU A 686 -40.050 21.657 -0.897 1.00 19.87 C

ANISOU 2949 C LEU A 686 2911 2387 2250 189 -839 -3 C

ATOM 2950 O LEU A 686 -41.068 21.051 -1.232 1.00 20.62 O

ANISOU 2950 O LEU A 686 2995 2465 2375 175 -905 -16 O

ATOM 2951 N ALA A 687 -39.063 21.085 -0.225 1.00 16.71 N

ANISOU 2951 N ALA A 687 2523 1991 1836 182 -788 -10 N

ATOM 2952 CA ALA A 687 -39.175 19.714 0.249 1.00 16.30 C

ANISOU 2952 CA ALA A 687 2469 1921 1803 156 -803 -31 C

ATOM 2953 CB ALA A 687 -38.224 18.804 -0.516 1.00 18.29 C

ANISOU 2953 CB ALA A 687 2795 2167 1986 176 -810 -51 C

ATOM 2954 C ALA A 687 -38.871 19.708 1.735 1.00 15.88 C

ANISOU 2954 C ALA A 687 2370 1872 1791 132 -739 -23 C

ATOM 2955 O ALA A 687 -37.729 19.914 2.144 1.00 12.89 O

ANISOU 2955 O ALA A 687 2007 1508 1383 142 -681 -17 O

ATOM 2956 N TYR A 688 -39.903 19.494 2.546 1.00 14.09 N

ANISOU 2956 N TYR A 688 2087 1633 1635 100 -749 -21 N

ATOM 2957 CA TYR A 688 -39.785 19.672 3.993 1.00 13.61 C

ANISOU 2957 CA TYR A 688 1980 1574 1617 78 -688 -9 C

ATOM 2958 CB TYR A 688 -41.148 20.029 4.587 1.00 19.70 C

ANISOU 2958 CB TYR A 688 2684 2334 2467 53 -701 3 C

ATOM 2959 CG TYR A 688 -41.592 21.458 4.415 1.00 17.29 C

ANISOU 2959 CG TYR A 688 2350 2043 2177 66 -694 27 C

ATOM 2960 CDl TYR A 688 -40.756 22.424 3.849 1.00 11.64 C

ANISOU 2960 CDl TYR A 688 1667 1349 1406 98 -672 38 C

ATOM 2961 CE1 TYR A 688 -41.186 23.738 3.700 1.00 10.00 C

ANISOU 2961 CE1 TYR A 688 1434 1152 1212 110 -665 61 C

ATOM 2962 CD2 TYR A 688 -42.860 21.845 4.830 1.00 16.44 C

ANISOU 2962 CD2 TYR A 688 2181 1926 2141 48 -708 40 C

ATOM 2963 CE2 TYR A 688 -43.292 23.144 4.697 1.00 18.27 C

ANISOU 2963 CE2 TYR A 688 2386 2169 2387 62 -701 63 C

ATOM 2964 CZ TYR A 688 -42.460 24.089 4.135 1.00 19.12 C

ANISOU 2964 CZ TYR A 688 2529 2297 2437 93 -680 73 C

ATOM 2965 OH TYR A 688 -42.927 25.376 4.012 1.00 19.57 O

ANISOU 2965 OH TYR A 688 2562 2363 2510 107 -672 96 O

ATOM 2966 C TYR A 688 -39.291 18.441 4.741 1.00 8.98 C

ANISOU 2966 C TYR A 688 1406 975 1032 60 -668 -25 C

ATOM 2967 O TYR A 688 -39.864 17.362 4.610 1.00 15.64 O

ANISOU 2967 O TYR A 688 2253 1795 1894 43 -709 -44 O

ATOM 2968 N MET A 689 -38.249 18.623 5.549 1.00 13.39 N

ANISOU 2968 N MET A 689 1970 1546 1573 64 -606 -19 N

ATOM 2969 CA MET A 689 -37.940 17.698 6.625 1.00 9.69 C ANISOU 2969 CA MET A 689 1497 1064 1121 45 -576 -27 C

ATOM 2970 CB MET A 689 -36.499 17.891 7.118 1.00 8.82 C

ANISOU 2970 CB MET A 689 1410 971 968 61 -518 -23 C

ATOM 2971 CG MET A 689 -35.462 17.420 6.107 1.00 12.80 C

ANISOU 2971 CG MET A 689 1974 1484 1405 89 -529 -37 C

ATOM 2972 SD MET A 689 -35.455 15.620 5.978 1.00 17.37 S

ANISOU 2972 SD MET A 689 2589 2037 1973 80 -562 -65 S

ATOM 2973 CE MET A 689 -34.610 15.173 7.485 1.00 12.07 C

ANISOU 2973 CE MET A 689 1909 1365 1312 69 -501 -64 C

ATOM 2974 C MET A 689 -38.910 18.035 7.745 1.00 10.40 C

ANISOU 2974 C MET A 689 1527 1143 1282 16 -556 -14 C

ATOM 2975 O MET A 689 -39.353 19.177 7.853 1.00 15.14 O

ANISOU 2975 O MET A 689 2094 1753 1905 19 -544 6 O

ATOM 2976 N PRO A 690 -39.240 17.050 8.591 1.00 13.87 N

ANISOU 2976 N PRO A 690 1954 1559 1756 -9 -548 -23 N

ATOM 2977 CD PRO A 690 -38.709 15.676 8.634 1.00 17.25 C

ANISOU 2977 CD PRO A 690 2421 1973 2160 -13 -555 -45 C

ATOM 2978 CA PRO A 690 -40.348 17.251 9.540 1.00 12.50 C

ANISOU 2978 CA PRO A 690 1724 1370 1656 -37 -534 -11 C

ATOM 2979 CB PRO A 690 -40.663 15.824 10.017 1.00 17.86 C

ANISOU 2979 CB PRO A 690 2408 2019 2359 -62 -543 -28 C

ATOM 2980 CG PRO A 690 -39.379 15.080 9.859 1.00 17.90 C

ANISOU 2980 CG PRO A 690 2471 2031 2301 -45 -533 -44 C

ATOM 2981 C PRO A 690 -40.019 18.158 10.727 1.00 19.65 C

ANISOU 2981 C PRO A 690 2607 2285 2576 -38 -468 10 C

ATOM 2982 0 PRO A 690 -40.935 18.711 11.329 1.00 16.35 O

ANISOU 2982 O PRO A 690 2142 1857 2213 -53 -453 26 O

ATOM 2983 N HIS A 691 -38.743 18.305 11.067 1.00 13.56 N

ANISOU 2983 N HIS A 691 1867 1530 1757 -22 -429 11 N

ATOM 2984 CA HIS A 691 -38.362 19.199 12.161 1.00 14.94 C

ANISOU 2984 CA HIS A 691 2024 1712 1941 -23 -370 29 C

ATOM 2985 CB HIS A 691 -37.713 18.411 13.298 1.00 13.51 C

ANISOU 2985 CB HIS A 691 1860 1519 1754 -32 -333 22 C

ATOM 2986 CG HIS A 691 -38.647 17.410 13.910 1.00 24.47 C

ANISOU 2986 CG HIS A 691 3232 2875 3191 -59 -339 15 C

ATOM 2987 CD2 HIS A 691 -39.686 17.570 14.764 1.00 22.53 C

ANISOU 2987 CD2 HIS A 691 2947 2609 3006 -81 -319 27 C

ATOM 2988 ND1 HIS A 691 -38.610 16.069 13.599 1.00 23.85 N

ANISOU 2988 ND1 HIS A 691 3179 2781 3103 -65 -368 -6 N

ATOM 2989 CE1 HIS A 691 -39.567 15.439 14.258 1.00 26.79 C

ANISOU 2989 CE1 HIS A 691 3528 3123 3529 -92 -365 -7 C

ATOM 2990 NE2 HIS A 691 -40.233 16.327 14.973 1.00 28.38 N

ANISOU 2990 NE2 HIS A 691 3689 3321 3774 -102 -334 14 N

ATOM 2991 C HIS A 691 -37.492 20.340 11.642 1.00 17.02 C

ANISOU 2991 C HIS A 691 2302 2005 2160 3 -356 39 C

ATOM 2992 O HIS A 691 -38.018 21.376 11.228 1.00 14.09 O ANISOU 2992 O HIS A 691 1909 1643 1802 9 -362 54 O

ATOM 2993 N THR A 692 -36.177 20.162 11.628 1.00 11.15 N

ANISOU 2993 N THR A 692 1594 1276 1367 19 -336 32 N

ATOM 2994 CA THR A 692 -35.349 21.134 10.893 1.00 9.04 C

ANISOU 2994 CA THR A 692 1343 1034 1056 44 -328 40 C

ATOM 2995 CB THR A 692 -34.421 21.975 11.818 1.00 10.78 C

ANISOU 2995 CB THR A 692 1560 1268 1267 47 -273 53 C

ATOM 2996 OG1 THR A 692 -33.651 22.897 11.030 1.00 15.50 O

ANISOU 2996 OG1 THR A 692 2172 1889 1827 69 -264 60 O

ATOM 2997 CG2 THR A 692 -33.480 21.105 12.618 1.00 10.75 C

ANISOU 2997 CG2 THR A 692 1576 1261 1247 44 -251 41 C

ATOM 2998 C THR A 692 -34.565 20.413 9.795 1.00 9.54 C

ANISOU 2998 C THR A 692 1452 1105 1067 65 -354 23 C

ATOM 2999 O THR A 692 -34.341 19.216 9.896 1.00 10.85 O

ANISOU 2999 O THR A 692 1639 1259 1224 61 -366 6 O

ATOM 3000 N PHE A 693 -34.167 21.133 8.744 1.00 10.78 N

ANISOU 3000 N PHE A 693 1627 1280 1188 88 -362 29 N

ATOM 3001 CA PHE A 693 -33.295 20.536 7.734 1.00 12.23 C

ANISOU 3001 CA PHE A 693 1858 1470 1317 112 -378 15 C

ATOM 3002 CB PHE A 693 -33.378 21.277 6.398 1.00 9.04 C

ANISOU 3002 CB PHE A 693 1474 1077 882 135 -400 21 C

ATOM 3003 CG PHE A 693 -32.548 22.520 6.340 1.00 12.60 C

ANISOU 3003 CG PHE A 693 1925 1550 1313 151 -357 38 C

ATOM 3004 CD1 PHE A 693 -31.293 22.511 5.742 1.00 9.50 C

ANISOU 3004 CD 1 PHE A 693 1569 1170 870 176 -337 36 C

ATOM 3005 CD2 PHE A 693 -33.021 23.710 6.883 1.00 15.40 C ANISOU 3005 CD2 PHE A 693 2242 1909 1699 142 -336 58 C

ATOM 3006 CE1 PHE A 693 -30.519 23.682 5.704 1.00 12.10 C

ANISOU 3006 CE1 PHE A 693 1895 1517 1184 189 -295 52 C

ATOM 3007 CE2 PHE A 693 -32.270 24.863 6.831 1.00 10.02 C

ANISOU 3007 CE2 PHE A 693 1563 1246 1001 155 -297 73 C

ATOM 3008 CZ PHE A 693 -31.024 24.860 6.259 1.00 10.84 C

ANISOU 3008 CZ PHE A 693 1699 1361 1057 177 -276 71 C

ATOM 3009 C PHE A 693 -31.867 20.568 8.250 1.00 13.52 C

ANISOU 3009 C PHE A 693 2036 1648 1452 122 -331 15 C

ATOM 3010 O PHE A 693 -30.979 19.895 7.715 1.00 12.17 O

ANISOU 3010 O PHE A 693 1902 1481 1241 141 -332 4 O

ATOM 3011 N PHE A 694 -31.638 21.371 9.285 1.00 10.38 N

ANISOU 3011 N PHE A 694 1609 1258 1077 112 -290 29 N

ATOM 3012 CA PHE A 694 -30.293 21.437 9.832 1.00 11.75 C

ANISOU 3012 CA PHE A 694 1791 1444 1228 120 -250 30 C

ATOM 3013 CB PHE A 694 -30.026 22.745 10.596 1.00 5.99 C

ANISOU 3013 CB PHE A 694 1035 727 516 114 -209 48 C

ATOM 3014 CG PHE A 694 -28.743 23.396 10.179 1.00 8.93 C

ANISOU 3014 CG PHE A 694 1420 1119 854 134 -181 54 C

ATOM 3015 CD1 PHE A 694 -27.579 23.210 10.925 1.00 9.41 C ANISOU 3015 CD1 PHE A 694 1481 1187 907 135 -152 50 C

ATOM 3016 CD2 PHE A 694 -28.671 24.115 8.981 1.00 15.60 C ANISOU 3016 CD2 PHE A 694 2278 1974 1674 153 -186 61 C

ATOM 3017 CE1 PHE A 694 -26.356 23.774 10.517 1.00 11.42 C

ANISOU 3017 CE1 PHE A 694 1744 1460 1135 153 -125 55 C

ATOM 3018 CE2 PHE A 694 -27.461 24.678 8.558 1.00 12.70 C

ANISOU 3018 CE2 PHE A 694 1924 1624 1277 172 -156 67 C

ATOM 3019 CZ PHE A 694 -26.299 24.504 9.324 1.00 14.63 C

ANISOU 3019 CZ PHE A 694 2164 1877 1520 170 -125 64 C

ATOM 3020 C PHE A 694 -29.935 20.175 10.623 1.00 12.82 C

ANISOU 3020 C PHE A 694 1937 1568 1367 112 -247 15 C

ATOM 3021 O PHE A 694 -30.811 19.514 11.210 1.00 9.96 O

ANISOU 3021 O PHE A 694 1564 1186 1037 92 -262 9 O

ATOM 3022 N ILE A 695 -28.655 19.811 10.581 1.00 9.24 N

ANISOU 3022 N ILE A 695 1505 1125 881 130 -229 8 N

ATOM 3023 CA ILE A 695 -28.145 18.678 11.347 1.00 9.14 C

ANISOU 3023 CA ILE A 695 1504 1102 865 127 -224 -5 C

ATOM 3024 CB ILE A 695 -28.242 17.360 10.523 1.00 12.10 C

ANISOU 3024 CB ILE A 695 1915 1464 1217 137 -257 -24 C

ATOM 3025 CG2 ILE A 695 -27.401 17.456 9.218 1.00 11.79 C

ANISOU 3025 CG2 ILE A 695 1907 1440 1131 168 -259 -26 C

ATOM 3026 CGI ILE A 695 -27.865 16.138 11.371 1.00 10.77 C

ANISOU 3026 CGI ILE A 695 1760 1282 1049 133 -252 -37 C

ATOM 3027 CD1 ILE A 695 -28.799 15.880 12.574 1.00 11.20 C

ANISOU 3027 CD 1 ILE A 695 1792 1316 1148 103 -251 -35 C

ATOM 3028 C ILE A 695 -26.689 18.992 11.725 1.00 9.91 C

ANISOU 3028 C ILE A 695 1603 1218 942 142 -188 -1 C

ATOM 3029 O ILE A 695 -26.083 19.891 11.160 1.00 13.13 O

ANISOU 3029 O ILE A 695 2010 1645 1335 155 -172 8 O

ATOM 3030 N GLY A 696 -26.144 18.279 12.694 1.00 6.49 N

ANISOU 3030 N GLY A 696 1173 779 512 139 -176 -9 N

ATOM 3031 CA GLY A 696 -24.750 18.459 13.065 1.00 10.04 C

ANISOU 3031 CA GLY A 696 1622 1245 946 153 -149 -7 C

ATOM 3032 C GLY A 696 -24.211 17.156 13.625 1.00 6.66 C

ANISOU 3032 C GLY A 696 1215 808 510 160 -152 -21 C

ATOM 3033 O GLY A 696 -24.962 16.338 14.150 1.00 11.18 O

ANISOU 3033 O GLY A 696 1794 1358 1097 146 -166 -29 O

ATOM 3034 N ASP A 697 -22.907 16.956 13.537 1.00 7.37 N

ANISOU 3034 N ASP A 697 1312 911 577 182 -137 -24 N

ATOM 3035 CA ASP A 697 -22.346 15.683 13.978 1.00 11.08 C

ANISOU 3035 CA ASP A 697 1802 1371 1035 193 -141 -37 C

ATOM 3036 CB ASP A 697 -21.243 15.220 13.019 1.00 8.32 C

ANISOU 3036 CB ASP A 697 1473 1032 656 225 -135 -42 C

ATOM 3037 CG ASP A 697 -20.984 13.730 13.114 1.00 7.57 C

ANISOU 3037 CG ASP A 697 1408 921 546 239 -146 -57 C

ATOM 3038 OD1 ASP A 697 -21.961 12.941 13.096 1.00 10.77 O ANISOU 3038 OD1 ASP A 697 1835 1306 952 226 -170 -67 O

ATOM 3039 OD2 ASP A 697 -19.802 13.355 13.207 1.00 9.52 O

ANISOU 3039 OD2 ASP A 697 1659 1176 781 262 -131 -59 O

ATOM 3040 C ASP A 697 -21.825 15.736 15.410 1.00 8.15 C

ANISOU 3040 C ASP A 697 1418 999 680 185 -125 -35 C

ATOM 3041 O ASP A 697 -21.019 14.911 15.812 1.00 10.62 O

ANISOU 3041 O ASP A 697 1742 1309 985 200 -123 -43 O

ATOM 3042 N HIS A 698 -22.329 16.680 16.195 1.00 8.06 N

ANISOU 3042 N HIS A 698 1381 986 694 163 -116 -25 N

ATOM 3043 CA HIS A 698 -21.805 16.903 17.545 1.00 8.22 C

ANISOU 3043 CA HIS A 698 1392 1006 726 157 -101 -22 C

ATOM 3044 CB HIS A 698 -22.512 18.096 18.185 1.00 9.24 C

ANISOU 3044 CB HIS A 698 1498 1131 881 132 -90 -9 C

ATOM 3045 CG HIS A 698 -22.355 19.354 17.392 1.00 8.22 C

ANISOU 3045 CG HIS A 698 1349 1024 753 133 -79 3 C

ATOM 3046 CD2 HIS A 698 -21.664 20.488 17.647 1.00 7.00 C

ANISOU 3046 CD2 HIS A 698 1174 885 603 131 -60 12 C

ATOM 3047 ND1 HIS A 698 -22.921 19.518 16.140 1.00 5.06 N

ANISOU 3047 ND1 HIS A 698 950 627 345 138 -89 5 N

ATOM 3048 CE1 HIS A 698 -22.589 20.708 15.667 1.00 11.97 C

ANISOU 3048 CE1 HIS A 698 1809 1520 1220 140 -74 16 C

ATOM 3049 NE2 HIS A 698 -21.826 21.314 16.562 1.00 7.60 N

ANISOU 3049 NE2 HIS A 698 1239 973 674 135 -55 21 N

ATOM 3050 C HIS A 698 -21.816 15.699 18.484 1.00 11.27 C

ANISOU 3050 C HIS A 698 1801 1371 1111 157 -108 -32 C

ATOM 3051 O HIS A 698 -20.883 15.526 19.272 1.00 8.39 O

ANISOU 3051 O HIS A 698 1436 1008 742 167 -102 -35 O

ATOM 3052 N ALA A 699 -22.860 14.875 18.417 1.00 10.21 N

ANISOU 3052 N ALA A 699 1684 1214 983 147 -122 -39 N

ATOM 3053 CA ALA A 699 -22.965 13.728 19.327 1.00 12.93 C

ANISOU 3053 CA ALA A 699 2052 1533 1327 145 -126 -48 C

ATOM 3054 CB ALA A 699 -24.338 13.050 19.211 1.00 15.18 C

ANISOU 3054 CB ALA A 699 2349 1790 1628 126 -138 -53 C

ATOM 3055 C ALA A 699 -21.851 12.721 19.056 1.00 16.37 C

ANISOU 3055 C ALA A 699 2511 1975 1735 174 -131 -59 C

ATOM 3056 O ALA A 699 -21.381 12.049 19.964 1.00 10.49 O

ANISOU 3056 O ALA A 699 1782 1219 985 182 -129 -64 O

ATOM 3057 N ASN A 700 -21.429 12.630 17.798 1.00 8.27 N

ANISOU 3057 N ASN A 700 1487 964 691 192 -137 -62 N

ATOM 3058 CA ASN A 700 -20.319 11.754 17.405 1.00 9.43 C

ANISOU 3058 CA ASN A 700 1652 1115 817 223 -138 -70 C

ATOM 3059 CB ASN A 700 -20.484 11.316 15.936 1.00 12.22 C

ANISOU 3059 CB ASN A 700 2025 1470 1149 237 -149 -76 C

ATOM 3060 CG ASN A 700 -19.314 10.468 15.432 1.00 19.02 C

ANISOU 3060 CG ASN A 700 2906 2335 1984 272 -145 -83 C

ATOM 3061 OD1 ASN A 700 -18.988 9.433 16.011 1.00 16.02 O ANISOU 3061 OD1 ASN A 700 2547 1941 1597 283 -148 -91 O

ATOM 3062 ND2 ASN A 700 -18.695 10.897 14.333 1.00 11.50 N ANISOU 3062 ND2 ASN A 700 1951 1403 1015 292 -136 -80 N

ATOM 3063 C ASN A 700 -18.935 12.397 17.599 1.00 9.99 C

ANISOU 3063 C ASN A 700 1700 1211 886 242 -121 -63 C

ATOM 3064 O ASN A 700 -18.003 11.742 18.053 1.00 10.74 O

ANISOU 3064 O ASN A 700 1803 1307 970 262 -120 -68 O

ATOM 3065 N MET A 701 -18.801 13.669 17.230 1.00 10.04 N

ANISOU 3065 N MET A 701 1678 1239 900 235 -110 -53 N

ATOM 3066 CA MET A 701 -17.510 14.352 17.328 1.00 10.35 C

ANISOU 3066 CA MET A 701 1693 1303 936 250 -95 -47 C

ATOM 3067 CB MET A 701 -17.467 15.584 16.416 1.00 7.49 C

ANISOU 3067 CB MET A 701 1309 962 575 246 -82 -36 C

ATOM 3068 CG MET A 701 -17.418 15.277 14.933 1.00 5.00 C

ANISOU 3068 CG MET A 701 1011 652 236 266 -81 -38 C

ATOM 3069 SD MET A 701 -17.525 16.762 13.915 1.00 10.99 S

ANISOU 3069 SD MET A 701 1750 1429 996 261 -64 -23 S

ATOM 3070 CE MET A 701 -15.978 17.583 14.308 1.00 6.71 C

ANISOU 3070 CE MET A 701 1171 911 467 271 -36 -14 C

ATOM 3071 C MET A 701 -17.170 14.778 18.746 1.00 7.07 C

ANISOU 3071 C MET A 701 1262 888 537 238 -93 -44 C

ATOM 3072 O MET A 701 -16.007 14.746 19.138 1.00 9.61 O

ANISOU 3072 O MET A 701 1574 1223 856 254 -90 -44 O

ATOM 3073 N PHE A 702 -18.173 15.208 19.510 1.00 10.10 N

ANISOU 3073 N PHE A 702 1644 1255 939 211 -94 -40 N

ATOM 3074 CA PHE A 702 -17.916 15.779 20.836 1.00 2.81 C

ANISOU 3074 CA PHE A 702 710 329 28 199 -90 -36 C

ATOM 3075 CB PHE A 702 -18.219 17.297 20.841 1.00 3.69 C

ANISOU 3075 CB PHE A 702 795 452 156 178 -78 -24 C

ATOM 3076 CG PHE A 702 -17.687 18.032 19.620 1.00 11.81 C

ANISOU 3076 CG PHE A 702 1801 1506 1179 187 -68 -17 C

ATOM 3077 CD1 PHE A 702 -16.319 18.116 19.384 1.00 10.73 C

ANISOU 3077 CD 1 PHE A 702 1649 1390 1039 206 -62 -18 C

ATOM 3078 CD2 PHE A 702 -18.562 18.640 18.723 1.00 10.90 C

ANISOU 3078 CD2 PHE A 702 1682 1392 1067 176 -63 -10 C

ATOM 3079 CE1 PHE A 702 -15.827 18.795 18.261 1.00 10.72 C

ANISOU 3079 CE1 PHE A 702 1629 1409 1036 215 -46 -11 C

ATOM 3080 CE2 PHE A 702 -18.088 19.328 17.601 1.00 5.65 C

ANISOU 3080 CE2 PHE A 702 1002 747 396 186 -51 -4 C

ATOM 3081 CZ PHE A 702 -16.712 19.401 17.377 1.00 11.08 C

ANISOU 3081 CZ PHE A 702 1676 1455 1080 205 -40 -3 C

ATOM 3082 C PHE A 702 -18.710 15.115 21.963 1.00 5.02 C

ANISOU 3082 C PHE A 702 1015 578 315 186 -96 -40 C

ATOM 3083 O PHE A 702 -19.383 15.809 22.733 1.00 7.42 O

ANISOU 3083 O PHE A 702 1316 871 632 164 -90 -33 O

ATOM 3084 N PRO A 703 -18.600 13.788 22.097 1.00 10.50 N ANISOU 3084 N PRO A 703 1737 1256 995 202 -106 -50 N

ATOM 3085 CD PRO A 703 -17.697 12.887 21.362 1.00 12.09 C

ANISOU 3085 CD PRO A 703 1948 1469 1178 232 -112 -58 C

ATOM 3086 CA PRO A 703 -19.353 13.081 23.143 1.00 12.79 C

ANISOU 3086 CA PRO A 703 2057 1516 1288 191 -108 -53 C

ATOM 3087 CB PRO A 703 -19.118 11.599 22.806 1.00 7.03 C

ANISOU 3087 CB PRO A 703 1356 774 540 212 -119 -64 C

ATOM 3088 CG PRO A 703 -17.810 11.574 22.126 1.00 10.22 C

ANISOU 3088 CG PRO A 703 1747 1205 932 240 -121 -67 C

ATOM 3089 C PRO A 703 -18.850 13.390 24.547 1.00 11.24 C

ANISOU 3089 C PRO A 703 1865 1312 1094 190 -106 -51 C

ATOM 3090 O PRO A 703 -19.576 13.161 25.518 1.00 8.16 O

ANISOU 3090 O PRO A 703 1498 895 706 177 -102 -50 O

ATOM 3091 N HIS A 704 -17.634 13.909 24.660 1.00 7.27 N

ANISOU 3091 N HIS A 704 1341 832 587 204 -110 -50 N

ATOM 3092 CA HIS A 704 -17.112 14.304 25.969 1.00 10.81 C

ANISOU 3092 CA HIS A 704 1795 1275 1036 203 -114 -49 C

ATOM 3093 CB HIS A 704 -15.598 14.585 25.916 1.00 12.37 C

ANISOU 3093 CB HIS A 704 1971 1503 1225 223 -126 -52 C

ATOM 3094 CG HIS A 704 -15.216 15.725 25.020 1.00 17.31 C

ANISOU 3094 CG HIS A 704 2555 2157 1863 216 -117 -45 C

ATOM 3095 CD2 HIS A 704 -14.503 16.855 25.263 1.00 3.61 C

ANISOU 3095 CD2 HIS A 704 790 439 142 209 -116 -39 C

ATOM 3096 ND1 HIS A 704 -15.549 15.762 23.680 1.00 9.43 N

ANISOU 3096 ND1 HIS A 704 1545 1171 865 217 -106 -42 N

ATOM 3097 CE1 HIS A 704 -15.083 16.877 23.143 1.00 8.53 C

ANISOU 3097 CE1 HIS A 704 1397 1080 764 212 -96 -34 C

ATOM 3098 NE2 HIS A 704 -14.438 17.556 24.078 1.00 8.95 N

ANISOU 3098 NE2 HIS A 704 1437 1137 827 206 -101 -33 N

ATOM 3099 C HIS A 704 -17.859 15.504 26.543 1.00 7.81 C

ANISOU 3099 C HIS A 704 1408 889 672 174 -102 -40 C

ATOM 3100 O HIS A 704 -17.712 15.808 27.721 1.00 15.43 O

ANISOU 3100 O HIS A 704 2387 1841 1636 169 -104 -39 O

ATOM 3101 N LEU A 705 -18.655 16.183 25.712 1.00 9.16 N

ANISOU 3101 N LEU A 705 1559 1066 854 157 -90 -33 N

ATOM 3102 CA LEU A 705 -19.430 17.350 26.163 1.00 7.79 C

ANISOU 3102 CA LEU A 705 1378 887 695 131 -75 -22 C

ATOM 3103 CB LEU A 705 -19.347 18.499 25.142 1.00 7.22 C

ANISOU 3103 CB LEU A 705 1270 842 632 124 -68 -14 C

ATOM 3104 CG LEU A 705 -17.934 18.901 24.672 1.00 7.26 C

ANISOU 3104 CG LEU A 705 1249 876 632 139 -73 -16 C

ATOM 3105 CD1 LEU A 705 -18.003 20.003 23.616 1.00 10.54 C

ANISOU 3105 CD 1 LEU A 705 1634 1313 1058 131 -61 -7 C

ATOM 3106 CD2 LEU A 705 -17.054 19.373 25.854 1.00 7.55 C

ANISOU 3106 CD2 LEU A 705 1286 913 670 138 -80 -17 C

ATOM 3107 C LEU A 705 -20.896 17.004 26.483 1.00 14.20 C ANISOU 3107 C LEU A 705 2211 1669 1516 114 -64 -19 C

ATOM 3108 O LEU A 705 -21.727 17.897 26.738 1.00 9.51 O

ANISOU 3108 O LEU A 705 1609 1066 939 93 -48 -9 O

ATOM 3109 N LYS A 706 -21.221 15.712 26.452 1.00 11.80 N

ANISOU 3109 N LYS A 706 1932 1348 1204 122 -70 -27 N

ATOM 3110 CA LYS A 706 -22.553 15.273 26.846 1.00 9.39 C

ANISOU 3110 CA LYS A 706 1645 1011 913 105 -58 -25 C

ATOM 3111 CB LYS A 706 -22.797 13.800 26.509 1.00 12.01 C

ANISOU 3111 CB LYS A 706 2000 1327 1236 114 -67 -35 C

ATOM 3112 CG LYS A 706 -22.926 13.504 25.039 1.00 23.68 C

ANISOU 3112 CG LYS A 706 3461 2822 2714 119 -80 -40 C

ATOM 3113 CD LYS A 706 -23.267 12.031 24.849 1.00 44.90 C

ANISOU 3113 CD LYS A 706 6178 5487 5394 125 -89 -51 C

ATOM 3114 CE LYS A 706 -22.595 11.455 23.613 1.00 48.12 C

ANISOU 3114 CE LYS A 706 6585 5915 5783 145 -106 -60 C

ATOM 3115 NZ LYS A 706 -22.979 12.184 22.369 1.00 23.17 N

ANISOU 3115 NZ LYS A 706 3397 2775 2631 138 -111 -56 N

ATOM 3116 C LYS A 706 -22.763 15.466 28.329 1.00 15.11 C

ANISOU 3116 C LYS A 706 2395 1707 1637 98 -43 -20 C

ATOM 3117 O LYS A 706 -23.878 15.697 28.769 1.00 19.55 O

ANISOU 3117 O LYS A 706 2963 2246 2219 79 -24 -12 O

ATOM 3118 N LYS A 707 -21.691 15.364 29.107 1.00 7.18 N

ANISOU 3118 N LYS A 707 1408 706 613 113 -53 -25 N

ATOM 3119 CA LYS A 707 -21.814 15.570 30.534 1.00 8.81 C

ANISOU 3119 CA LYS A 707 1647 886 815 109 -43 -22 C

ATOM 3120 CB LYS A 707 -21.620 14.251 31.298 1.00 13.16 C

ANISOU 3120 CB LYS A 707 2244 1411 1347 126 -48 -30 C

ATOM 3121 CG LYS A 707 -22.774 13.270 31.130 1.00 29.50 C

ANISOU 3121 CG LYS A 707 4329 3451 3426 117 -33 -30 C

ATOM 3122 CD LYS A 707 -22.544 12.019 31.957 1.00 41.50 C

ANISOU 3122 CD LYS A 707 5900 4944 4926 134 -35 -38 C

ATOM 3123 CE LYS A 707 -23.585 10.954 31.659 1.00 48.47 C

ANISOU 3123 CE LYS A 707 6796 5798 5820 125 -22 -39 C

ATOM 3124 NZ LYS A 707 -23.312 9.705 32.427 1.00 49.24 N

ANISOU 3124 NZ LYS A 707 6945 5870 5896 143 -23 -45 N

ATOM 3125 C LYS A 707 -20.757 16.556 30.948 1.00 13.35 C

ANISOU 3125 C LYS A 707 2211 1480 1381 114 -54 -21 C

ATOM 3126 O LYS A 707 -19.799 16.780 30.212 1.00 10.27 O

ANISOU 3126 O LYS A 707 1791 1121 989 124 -70 -25 O

ATOM 3127 N LYS A 708 -20.928 17.149 32.125 1.00 10.73 N

ANISOU 3127 N LYS A 708 1904 1127 1047 105 -43 -17 N

ATOM 3128 CA LYS A 708 -19.930 18.067 32.650 1.00 12.31 C

ANISOU 3128 CA LYS A 708 2098 1341 1238 108 -57 -18 C

ATOM 3129 CB LYS A 708 -20.211 19.508 32.168 1.00 13.39 C

ANISOU 3129 CB LYS A 708 2199 1493 1394 87 -44 -8 C

ATOM 3130 CG LYS A 708 -21.491 20.153 32.728 1.00 11.04 C ANISOU 3130 CG LYS A 708 1918 1168 1110 67 -12 4 C ATOM 3131 CD LYS A 708 -21.572 21.636 32.308 1.00 16.00 C

ANISOU 3131 CD LYS A 708 2513 1812 1754 50 -1 13 C

ATOM 3132 CE LYS A 708 -22.750 22.366 32.974 1.00 11.71 C

ANISOU 3132 CE LYS A 708 1987 1240 1223 32 32 26 C ATOM 3133 NZ LYS A 708 -24.059 21.947 32.409 1.00 12.16 N

ANISOU 3133 NZ LYS A 708 2033 1285 1301 24 53 34 N

ATOM 3134 C LYS A 708 -19.924 18.016 34.165 1.00 11.22 C

ANISOU 3134 C LYS A 708 2012 1170 1083 111 -56 -18 C

ATOM 3135 O LYS A 708 -20.895 17.566 34.773 1.00 15.67 O

ANISOU 3135 O LYS A 708 2610 1698 1645 106 -33 -14 O

ATOM 3136 N ALA A 709 -18.816 18.434 34.765 1.00 10.25 N

ANISOU 3136 N ALA A 709 1893 1054 946 119 -81 -24 N ATOM 3137 CA ALA A 709 -18.767 18.682 36.204 1.00 12.86 C

ANISOU 3137 CA ALA A 709 2274 1354 1258 120 -82 -25 C ATOM 3138 CB ALA A 709 -17.862 17.673 36.917 1.00 15.53 C ANISOU 3138 CB ALA A 709 2646 1683 1573 148 -112 -35 C

ATOM 3139 C ALA A 709 -18.229 20.088 36.371 1.00 17.73 C

ANISOU 3139 C ALA A 709 2871 1986 1880 107 -91 -23 C

ATOM 3140 O ALA A 709 -17.682 20.656 35.429 1.00 8.94 O

ANISOU 3140 O ALA A 709 1707 907 782 102 -100 -23 O

ATOM 3141 N VAL A 710 -18.404 20.666 37.547 1.00 8.54 N

ANISOU 3141 N VAL A 710 1750 793 702 101 -86 -21 N ATOM 3142 CA VAL A 710 -17.869 21.990 37.787 1.00 10.16 C

ANISOU 3142 CA VAL A 710 1942 1008 911 87 -97 -21 C ATOM 3143 CB VAL A 710 -18.958 23.075 37.778 1.00 14.36 C

ANISOU 3143 CB VAL A 710 2473 1526 1458 63 -57 -8 C ATOM 3144 CGI VAL A 710 -19.722 23.069 36.452 1.00 21.07 C

ANISOU 3144 CGI VAL A 710 3275 2396 2335 54 -33 1 C ATOM 3145 CG2 VAL A 710 -19.929 22.890 38.947 1.00 19.22 C

ANISOU 3145 CG2 VAL A 710 3153 2093 2056 63 -29 -2 C

ATOM 3146 C VAL A 710 -17.108 21.972 39.119 1.00 18.54 C

ANISOU 3146 C VAL A 710 3054 2048 1944 99 -127 -31 C

ATOM 3147 O VAL A 710 -17.267 21.060 39.931 1.00 19.14 O

ANISOU 3147 O VAL A 710 3181 2096 1996 115 -130 -34 O

ATOM 3148 N ILE A 711 -16.244 22.952 39.316 1.00 17.54 N

ANISOU 3148 N ILE A 711 2911 1934 1819 90 -153 -36 N

ATOM 3149 CA ILE A 711 -15.522 23.083 40.573 1.00 15.29 C

ANISOU 3149 CA ILE A 711 2673 1628 1507 99 -187 -46 C

ATOM 3150 CB ILE A 711 -14.011 23.260 40.342 1.00 27.85 C

ANISOU 3150 CB ILE A 711 4223 3253 3108 105 -238 -58 C ATOM 3151 CG2 ILE A 711 -13.322 23.690 41.623 1.00 36.95 C

ANISOU 3151 CG2 ILE A 711 5420 4382 4236 108 -277 -68 C ATOM 3152 CGI ILE A 711 -13.390 21.961 39.827 1.00 27.11 C

ANISOU 3152 CGI ILE A 711 4107 3179 3014 132 -259 -64 C ATOM 3153 CD1 ILE A 711 -11.893 22.027 39.709 1.00 30.80 C ANISOU 3153 CD1 ILE A 711 4536 3675 3492 142 -309 -75 C ATOM 3154 C ILE A 711 -16.054 24.331 41.248 1.00 26.34 C ANISOU 3154 C ILE A 711 4102 3002 2902 77 -168 -40 C ATOM 3155 O ILE A 711 -15.971 25.416 40.681 1.00 23.11 O ANISOU 3155 O ILE A 711 3653 2613 2516 57 -161 -36 O ATOM 3156 N ASP A 712 -16.619 24.177 42.443 1.00 30.39 N ANISOU 3156 N ASP A 712 4689 3471 3386 83 -156 -38 N ATOM 3157 CA ASP A 712 -17.134 25.319 43.190 1.00 29.56 C ANISOU 3157 CA ASP A 712 4622 3337 3272 66 -135 -33 C ATOM 3158 CB ASP A 712 -18.152 24.865 44.234 1.00 28.67 C ANISOU 3158 CB ASP A 712 4588 3173 3132 75 -100 -25 C ATOM 3159 CG ASP A 712 -18.556 25.985 45.177 1.00 47.57 C ANISOU 3159 CG ASP A 712 7035 5531 5509 63 -81 -21 C ATOM 3160 OD1 ASP A 712 -18.689 25.722 46.397 1.00 39.38 O ANISOU 3160 OD1 ASP A 712 6076 4450 4434 76 -81 -23 O ATOM 3161 OD2 ASP A 712 -18.724 27.132 44.696 1.00 40.39 O ANISOU 3161 OD2 ASP A 712 6090 4634 4621 41 -67 -16 O ATOM 3162 C ASP A 712 -15.983 26.060 43.867 1.00 41.96 C ANISOU 3162 C ASP A 712 6206 4908 4829 63 -185 -46 C ATOM 3163 O ASP A 712 -15.419 25.573 44.849 1.00 61.88 O ANISOU 3163 O ASP A 712 8780 7410 7320 81 -220 -57 O ATOM 3164 N PHE A 713 -15.640 27.234 43.346 1.00 51.60 N ANISOU 3164 N PHE A 713 8809 5256 5541 1198 -2736 683 N ATOM 3165 CA PHE A 713 -14.447 27.936 43.801 1.00 55.63 C ANISOU 3165 CA PHE A 713 9357 5763 6015 1150 -2817 713 C ATOM 3166 CB PHE A 713 -13.561 28.308 42.608 1.00 56.11 C ANISOU 3166 CB PHE A 713 9324 5883 6114 1138 -2862 733 C ATOM 3167 CG PHE A 713 -14.049 29.491 41.833 1.00 52.42 C ANISOU 3167 CG PHE A 713 8849 5416 5652 1138 -2842 716 C ATOM 3168 CD1 PHE A 713 -15.339 29.521 41.322 1.00 61.54 C ANISOU 3168 CD1 PHE A 713 9988 6565 6828 1177 -2764 682 C ATOM 3169 CD2 PHE A 713 -13.212 30.571 41.598 1.00 56.10 C ANISOU 3169 CD2 PHE A 713 9321 5893 6103 1097 -2901 737 C ATOM 3170 CE1 PHE A 713 -15.787 30.612 40.605 1.00 52.39 C ANISOU 3170 CE1 PHE A 713 8820 5410 5675 1180 -2743 671 C ATOM 3171 CE2 PHE A 713 -13.653 31.670 40.879 1.00 56.55 C ANISOU 3171 CE2 PHE A 713 9373 5949 6164 1098 -2880 722 C ATOM 3172 CZ PHE A 713 -14.942 31.696 40.384 1.00 44.24 C ANISOU 3172 CZ PHE A 713 7799 4384 4627 1142 -2800 689 C ATOM 3173 C PHE A 713 -14.740 29.163 44.668 1.00 73.57 C ANISOU 3173 C PHE A 713 11753 7976 8224 1121 -2820 708 C ATOM 3174 0 PHE A 713 -14.089 30.200 44.538 1.00 83.35 O ANISOU 3174 O PHE A 713 13013 9214 9440 1082 -2871 722 O ATOM 3175 N LYS A 714 -15.713 29.031 45.563 1.00 84.26 N ANISOU 3175 N LYS A 714 13192 9276 9546 1141 -2763 688 N ATOM 3176 CA LYS A 714 -16.053 30.098 46.499 1.00 79.73 C ANISOU 3176 CA LYS A 714 12753 8634 8905 1121 -2755 682 C

ATOM 3177 CB LYS A 714 -17.208 30.947 45.960 1.00 82.08 C ANISOU 3177 CB LYS A 714 13060 8915 9210 1155 -2680 659 C

ATOM 3178 CG LYS A 714 -16.991 31.497 44.558 1.00 84.74 C ANISOU 3178 CG LYS A 714 13297 9306 9594 1155 -2692 659 C

ATOM 3179 CD LYS A 714 -18.298 31.997 43.966 1.00 79.87 C ANISOU 3179 CD LYS A 714 12666 8684 8998 1201 -2606 640 C

ATOM 3180 CE LYS A 714 -19.417 30.978 44.164 1.00 72.63 C ANISOU 3180 CE LYS A 714 11727 7765 8106 1247 -2532 629 C

ATOM 3181 NZ LYS A 714 -19.087 29.633 43.612 1.00 46.45 N

ANISOU 3181 NZ LYS A 714 8304 4502 4842 1254 -2550 629 N

ATOM 3182 C LYS A 714 -16.436 29.505 47.850 1.00 63.94 C

ANISOU 3182 C LYS A 714 10851 6581 6861 1128 -2731 679 C

ATOM 3183 O LYS A 714 -17.355 28.687 47.941 1.00 46.01 O

ANISOU 3183 O LYS A 714 8561 4306 4614 1172 -2664 664 O

ATOM 3184 N ILE A 719 -23.636 28.185 43.567 1.00 35.82 N

ANISOU 3184 N ILE A 719 5765 4295 3550 464 927 247 N

ATOM 3185 CA ILE A 719 -23.074 27.197 42.656 1.00 36.61 C

ANISOU 3185 CA ILE A 719 5794 4425 3691 447 877 247 C

ATOM 3186 CB ILE A 719 -23.688 25.801 42.902 1.00 30.93 C

ANISOU 3186 CB ILE A 719 5047 3680 3023 459 939 272 C

ATOM 3187 CG2 ILE A 719 -23.367 24.860 41.755 1.00 45.85 C

ANISOU 3187 CG2 ILE A 719 6846 5598 4976 440 894 267 C

ATOM 3188 CGI ILE A 719 -23.178 25.238 44.226 1.00 33.75 C

ANISOU 3188 CGI ILE A 719 5494 4023 3307 479 963 298 C

ATOM 3189 CD1 ILE A 719 -24.006 24.097 44.753 1.00 26.43 C

ANISOU 3189 CD1 ILE A 719 4562 3057 2424 500 1050 325 C

ATOM 3190 C ILE A 719 -23.265 27.616 41.201 1.00 38.21 C

ANISOU 3190 C ILE A 719 5907 4651 3959 427 834 223 C

ATOM 3191 O ILE A 719 -24.393 27.766 40.730 1.00 39.76 O

ANISOU 3191 O ILE A 719 6052 4831 4225 433 877 217 O

ATOM 3192 N TYR A 720 -22.151 27.820 40.501 1.00 34.39 N

ANISOU 3192 N TYR A 720 5407 4208 3452 405 749 209 N

ATOM 3193 CA TYR A 720 -22.178 28.241 39.104 1.00 25.42 C

ANISOU 3193 CA TYR A 720 4194 3097 2368 388 702 187 C

ATOM 3194 CB TYR A 720 -21.115 29.310 38.843 1.00 24.97 C

ANISOU 3194 CB TYR A 720 4160 3057 2271 372 623 166 C

ATOM 3195 CG TYR A 720 -21.390 30.663 39.460 1.00 23.97 C

ANISOU 3195 CG TYR A 720 4093 2907 2108 381 643 156 C

ATOM 3196 CD1 TYR A 720 -22.653 31.233 39.400 1.00 38.63 C

ANISOU 3196 CD 1 TYR A 720 5942 4747 3990 396 708 156 C

ATOM 3197 CE1 TYR A 720 -22.903 32.476 39.952 1.00 55.69 C

ANISOU 3197 CE1 TYR A 720 8157 6885 6118 404 727 148 C

ATOM 3198 CD2 TYR A 720 -20.372 31.387 40.072 1.00 52.36 C

ANISOU 3198 CD2 TYR A 720 7748 6499 5649 375 596 145 C

ATOM 3199 CE2 TYR A 720 -20.611 32.632 40.625 1.00 64.55 C ANISOU 3199 CE2 TYR A 720 9345 8020 7159 382 614 135 C

ATOM 3200 CZ TYR A 720 -21.880 33.171 40.563 1.00 75.02 C

ANISOU 3200 CZ TYR A 720 10667 9330 8510 396 681 138 C

ATOM 3201 OH TYR A 720 -22.131 34.409 41.112 1.00 87.95 O ANISOU 3201 OH TYR A 720 12357 10944 10115 403 702 128 O

ATOM 3202 C TYR A 720 -21.895 27.041 38.212 1.00 25.27 C

ANISOU 3202 C TYR A 720 4098 3101 2403 375 670 189 C

ATOM 3203 O TYR A 720 -21.044 26.200 38.550 1.00 10.90 O

ANISOU 3203 O TYR A 720 2296 1292 553 369 645 202 O

ATOM 3204 N ASP A 721 -22.578 26.972 37.070 1.00 25.89 N

ANISOU 3204 N ASP A 721 4092 3186 2559 372 668 176 N

ATOM 3205 CA ASP A 721 -22.367 25.868 36.131 1.00 23.63 C

ANISOU 3205 CA ASP A 721 3727 2922 2329 359 637 174 C

ATOM 3206 CB ASP A 721 -23.700 25.359 35.559 1.00 11.76 C

ANISOU 3206 CB ASP A 721 2146 1403 921 370 687 168 C

ATOM 3207 CG ASP A 721 -24.361 26.357 34.595 1.00 25.96 C

ANISOU 3207 CG ASP A 721 3899 3209 2757 374 674 144 C

ATOM 3208 OD1 ASP A 721 -23.890 27.514 34.484 1.00 15.26 O

ANISOU 3208 OD1 ASP A 721 2580 1866 1353 371 639 135 O

ATOM 3209 OD2 ASP A 721 -25.363 25.981 33.943 1.00 15.47 O

ANISOU 3209 OD2 ASP A 721 2496 1873 1509 383 700 133 O

ATOM 3210 C ASP A 721 -21.427 26.218 34.979 1.00 17.42 C

ANISOU 3210 C ASP A 721 2904 2176 1537 338 551 156 C

ATOM 3211 O ASP A 721 -21.232 25.414 34.074 1.00 19.69 O

ANISOU 3211 O ASP A 721 3124 2484 1871 328 520 151 O

ATOM 3212 N ASN A 722 -20.845 27.408 34.994 1.00 16.38 N

ANISOU 3212 N ASN A 722 2817 2055 1352 333 516 145 N

ATOM 3213 CA ASN A 722 -20.130 27.852 33.799 1.00 19.67 C

ANISOU 3213 CA ASN A 722 3195 2505 1774 316 445 126 C

ATOM 3214 CB ASN A 722 -21.099 28.517 32.814 1.00 7.88 C

ANISOU 3214 CB ASN A 722 1647 1012 336 326 455 110 C

ATOM 3215 CG ASN A 722 -21.760 29.765 33.394 1.00 12.71 C

ANISOU 3215 CG ASN A 722 2308 1599 923 341 497 107 C

ATOM 3216 OD1 ASN A 722 -21.485 30.155 34.522 1.00 9.42 O

ANISOU 3216 OD1 ASN A 722 1968 1166 447 343 517 115 O

ATOM 3217 ND2 ASN A 722 -22.646 30.383 32.617 1.00 8.82 N

ANISOU 3217 ND2 ASN A 722 1772 1104 475 354 509 94 N

ATOM 3218 C ASN A 722 -18.918 28.743 34.088 1.00 13.56 C

ANISOU 3218 C ASN A 722 2470 1729 954 302 385 116 C

ATOM 3219 O ASN A 722 -18.498 29.559 33.255 1.00 12.22 O

ANISOU 3219 O ASN A 722 2279 1569 793 292 339 99 O

ATOM 3220 N ARG A 723 -18.354 28.555 35.276 1.00 11.80 N

ANISOU 3220 N ARG A 723 2309 1488 686 303 387 126 N

ATOM 3221 CA ARG A 723 -17.161 29.283 35.698 1.00 15.97 C

ANISOU 3221 CA ARG A 723 2882 2011 1174 291 333 112 C

ATOM 3222 CB ARG A 723 -17.297 29.704 37.159 1.00 17.75 C ANISOU 3222 CB ARG A 723 3192 2208 1344 306 372 119 C

ATOM 3223 CG ARG A 723 -17.792 31.124 37.338 1.00 22.37 C

ANISOU 3223 CG ARG A 723 3812 2776 1912 313 394 107 C

ATOM 3224 CD ARG A 723 -19.123 31.364 36.638 1.00 19.19 C

ANISOU 3224 CD ARG A 723 3367 2372 1551 325 443 110 C

ATOM 3225 NE ARG A 723 -19.621 32.711 36.949 1.00 35.93 N

ANISOU 3225 NE ARG A 723 5528 4472 3652 334 471 101 N

ATOM 3226 CZ ARG A 723 -20.864 33.136 36.726 1.00 35.50 C

ANISOU 3226 CZ ARG A 723 5459 4407 3621 350 527 103 C

ATOM 3227 NH1 ARG A 723 -21.768 32.324 36.193 1.00 19.33 N

ANISOU 3227 NH1 ARG A 723 3356 2369 1619 359 564 111 N

ATOM 3228 NH2 ARG A 723 -21.208 34.379 37.048 1.00 41.74 N

ANISOU 3228 NH2 ARG A 723 6289 5178 4391 357 549 94 N

ATOM 3229 C ARG A 723 -15.918 28.423 35.534 1.00 11.94 C

ANISOU 3229 C ARG A 723 2353 1519 667 273 274 111 C

ATOM 3230 O ARG A 723 -14.954 28.833 34.895 1.00 13.86 O

ANISOU 3230 O ARG A 723 2573 1773 919 254 214 93 O

ATOM 3231 N AILE A 724 -15.949 27.233 36.129 0.50 10.49 N

ANISOU 3231 N AILE A 724 2178 1334 476 281 296 130 N

ATOM 3232 CA AILE A 724 -14.868 26.258 35.995 0.50 14.76 C

ANISOU 3232 CA AILE A 724 2696 1890 1020 267 247 132 C

ATOM 3233 CB AILE A 724 -14.037 26.133 37.284 0.50 18.92 C

ANISOU 3233 CB AILE A 724 3294 2406 1491 274 235 136 C

ATOM 3234 CG2AILE A 724 -12.892 25.146 37.079 0.50 15.12 C

ANISOU 3234 CG2AILE A 724 2786 1942 1018 259 183 136 C

ATOM 3235 CGI AILE A 724 -13.507 27.500 37.721 0.50 17.87 C

ANISOU 3235 CGI AILE A 724 3210 2260 1319 270 210 114 C

ATOM 3236 CD 1 AILE A 724 -13.152 27.582 39.204 0.50 8.23 C

ANISOU 3236 CD 1 AILE A 724 2074 1022 31 287 220 119 C

ATOM 3237 C AILE A 724 -15.482 24.903 35.697 0.50 13.40 C

ANISOU 3237 C AILE A 724 2480 1728 882 272 281 153 C

ATOM 3238 O AILE A 724 -16.152 24.329 36.551 0.50 7.21 O

ANISOU 3238 O AILE A 724 1730 928 83 292 342 175 O

ATOM 3239 N BILE A 724 -15.943 27.247 36.157 0.50 11.03 N

ANISOU 3239 N BILE A 724 2247 1401 542 281 296 130 N

ATOM 3240 CA BILE A 724 -14.891 26.248 35.993 0.50 14.30 C

ANISOU 3240 CA BILE A 724 2638 1832 963 267 248 132 C

ATOM 3241 CB BILE A 724 -14.068 26.032 37.271 0.50 17.18 C

ANISOU 3241 CB BILE A 724 3070 2185 1271 274 237 137 C

ATOM 3242 CG2BILE A 724 -12.911 25.074 36.995 0.50 10.70 C

ANISOU 3242 CG2BILE A 724 2221 1384 462 259 182 137 C

ATOM 3243 CG1BILE A 724 -13.567 27.365 37.820 0.50 19.83 C

ANISOU 3243 CG1BILE A 724 3462 2508 1566 272 215 118 C

ATOM 3244 CD 1 BILE A 724 -12.944 28.243 36.778 0.50 7.40 C

ANISOU 3244 CD 1BILE A 724 1847 945 20 248 162 93 C

ATOM 3245 C BILE A 724 -15.552 24.933 35.662 0.50 12.94 C ANISOU 3245 C BILE A 724 2421 1670 826 273 283 153 C

ATOM 3246 O BILE A 724 -16.326 24.409 36.458 0.50 16.28 O

ANISOU 3246 O BILE A 724 2873 2075 1236 292 348 174 O

ATOM 3247 N VAL A 725 -15.226 24.392 34.493 1.00 10.42 N

ANISOU 3247 N VAL A 725 2030 1376 552 256 245 146 N

ATOM 3248 CA VAL A 725 -15.938 23.245 33.967 1.00 10.37 C

ANISOU 3248 CA VAL A 725 1972 1382 588 258 278 161 C

ATOM 3249 CB VAL A 725 -16.683 23.641 32.662 1.00 8.39 C

ANISOU 3249 CB VAL A 725 1656 1149 383 255 279 147 C

ATOM 3250 CGI VAL A 725 -17.483 22.442 32.095 1.00 6.85 C

ANISOU 3250 CGI VAL A 725 1394 961 249 258 314 156 C

ATOM 3251 CG2 VAL A 725 -17.592 24.870 32.895 1.00 10.62 C

ANISOU 3251 CG2 VAL A 725 1968 1415 653 270 319 140 C

ATOM 3252 C VAL A 725 -14.992 22.108 33.616 1.00 6.80 C

ANISOU 3252 C VAL A 725 1485 948 152 243 234 166 C

ATOM 3253 O VAL A 725 -13.887 22.344 33.100 1.00 12.75 O

ANISOU 3253 O VAL A 725 2220 1714 909 224 167 148 O

ATOM 3254 N LEU A 726 -15.409 20.879 33.905 1.00 6.13 N

ANISOU 3254 N LEU A 726 1390 862 79 251 277 189 N

ATOM 3255 CA LEU A 726 -14.643 19.698 33.481 1.00 6.17 C

ANISOU 3255 CA LEU A 726 1355 885 106 237 243 195 C

ATOM 3256 CB LEU A 726 -14.275 18.818 34.674 1.00 6.78 C

ANISOU 3256 CB LEU A 726 1482 945 148 249 266 219 C

ATOM 3257 CG LEU A 726 -13.394 19.302 35.840 1.00 28.65 C

ANISOU 3257 CG LEU A 726 4330 3700 2856 258 242 217 C

ATOM 3258 CD1 LEU A 726 -13.434 18.290 36.968 1.00 30.17 C

ANISOU 3258 CD 1 LEU A 726 4569 3876 3018 280 287 247 C

ATOM 3259 CD2 LEU A 726 -11.958 19.523 35.439 1.00 21.53 C

ANISOU 3259 CD2 LEU A 726 3412 2815 1951 236 157 194 C

ATOM 3260 C LEU A 726 -15.507 18.872 32.524 1.00 10.51 C

ANISOU 3260 C LEU A 726 1829 1447 717 234 274 199 C

ATOM 3261 O LEU A 726 -16.715 18.767 32.726 1.00 8.41 O

ANISOU 3261 O LEU A 726 1548 1156 493 250 338 202 O

ATOM 3262 N ASN A 727 -14.881 18.295 31.496 1.00 10.52 N

ANISOU 3262 N ASN A 727 1771 1475 749 214 222 191 N

ATOM 3263 CA ASN A 727 -15.511 17.331 30.597 1.00 10.62 C

ANISOU 3263 CA ASN A 727 1698 1491 847 211 237 186 C

ATOM 3264 CB ASN A 727 -15.896 17.946 29.241 1.00 9.99 C

ANISOU 3264 CB ASN A 727 1555 1430 812 205 207 158 C

ATOM 3265 CG ASN A 727 -16.757 19.182 29.358 1.00 9.51 C

ANISOU 3265 CG ASN A 727 1514 1355 743 221 234 147 C

ATOM 3266 OD1 ASN A 727 -16.257 20.302 29.348 1.00 13.50 O ANISOU 3266 OD1 ASN A 727 2062 1870 1199 217 201 139 O

ATOM 3267 ND2 ASN A 727 -18.067 18.986 29.431 1.00 7.57 N

ANISOU 3267 ND2 ASN A 727 1237 1086 551 237 294 144 N

ATOM 3268 C ASN A 727 -14.503 16.209 30.292 1.00 6.62 C ANISOU 3268 C ASN A 727 1166 1003 345 194 197 195 C

ATOM 3269 O ASN A 727 -13.300 16.451 30.099 1.00 8.71 O

ANISOU 3269 O ASN A 727 1448 1289 572 178 134 190 O

ATOM 3270 N GLY A 728 -14.994 14.987 30.203 1.00 9.94 N

ANISOU 3270 N GLY A 728 1540 1413 824 196 234 203 N

ATOM 3271 CA GLY A 728 -14.164 13.925 29.682 1.00 5.57 C

ANISOU 3271 CA GLY A 728 948 879 290 179 197 208 C

ATOM 3272 C GLY A 728 -14.872 12.605 29.629 1.00 7.13 C

ANISOU 3272 C GLY A 728 1092 1058 558 183 249 216 C

ATOM 3273 O GLY A 728 -15.766 12.330 30.435 1.00 11.09 O

ANISOU 3273 O GLY A 728 1611 1527 1075 202 321 228 O

ATOM 3274 N ILE A 729 -14.464 11.786 28.667 1.00 12.38 N

ANISOU 3274 N ILE A 729 1692 1744 1268 166 214 207 N

ATOM 3275 CA ILE A 729 -14.925 10.405 28.589 1.00 15.54 C

ANISOU 3275 CA ILE A 729 2040 2129 1736 166 258 214 C

ATOM 3276 CB ILE A 729 -14.120 9.620 27.530 1.00 9.93 C

ANISOU 3276 CB ILE A 729 1269 1448 1056 143 202 205 C

ATOM 3277 CG2 ILE A 729 -14.506 8.131 27.541 1.00 20.97 C

ANISOU 3277 CG2 ILE A 729 2617 2828 2521 143 249 214 C

ATOM 3278 CGI ILE A 729 -14.331 10.259 26.153 1.00 18.32 C

ANISOU 3278 CGI ILE A 729 2272 2538 2152 134 155 171 C

ATOM 3279 CD1 ILE A 729 -15.784 10.519 25.824 1.00 14.52 C

ANISOU 3279 CD 1 ILE A 729 1744 2040 1731 149 201 150 C

ATOM 3280 C ILE A 729 -14.809 9.698 29.938 1.00 17.99 C

ANISOU 3280 C ILE A 729 2410 2411 2016 180 310 249 C

ATOM 3281 O ILE A 729 -15.702 8.958 30.329 1.00 12.56 O

ANISOU 3281 O ILE A 729 1703 1692 1376 192 382 258 O

ATOM 3282 N ASP A 730 -13.704 9.919 30.646 1.00 11.87 N

ANISOU 3282 N ASP A 730 1706 1646 1159 180 276 268 N

ATOM 3283 CA ASP A 730 -13.502 9.265 31.946 1.00 13.74 C

ANISOU 3283 CA ASP A 730 2007 1858 1356 198 320 302 C

ATOM 3284 CB ASP A 730 -12.083 8.704 32.009 1.00 14.95 C

ANISOU 3284 CB ASP A 730 2180 2034 1467 187 263 316 C

ATOM 3285 CG ASP A 730 -11.781 7.793 30.834 1.00 21.17 C

ANISOU 3285 CG ASP A 730 2882 2841 2321 164 232 304 C

ATOM 3286 OD1 ASP A 730 -12.513 6.802 30.661 1.00 12.75 O ANISOU 3286 OD1 ASP A 730 1765 1755 1324 167 285 308 O

ATOM 3287 OD2 ASP A 730 -10.833 8.076 30.070 1.00 20.72 O ANISOU 3287 OD2 ASP A 730 2807 2817 2248 143 157 290 O

ATOM 3288 C ASP A 730 -13.790 10.146 33.180 1.00 14.03 C

ANISOU 3288 C ASP A 730 2134 1873 1326 222 355 315 C

ATOM 3289 0 ASP A 730 -13.289 9.884 34.269 1.00 11.06 O

ANISOU 3289 O ASP A 730 1827 1485 889 239 369 341 O

ATOM 3290 N LEU A 731 -14.600 11.183 33.012 1.00 13.25 N

ANISOU 3290 N LEU A 731 2032 1768 1235 227 370 296 N

ATOM 3291 CA LEU A 731 -14.880 12.107 34.118 1.00 12.31 C ANISOU 3291 CA LEU A 731 1996 1629 1052 248 400 305 C

ATOM 3292 CB LEU A 731 -15.761 13.263 33.645 1.00 15.48 C

ANISOU 3292 CB LEU A 731 2378 2028 1474 248 408 280 C

ATOM 3293 CG LEU A 731 -16.137 14.293 34.737 1.00 10.09 C

ANISOU 3293 CG LEU A 731 1780 1324 731 269 443 287 C

ATOM 3294 CD1 LEU A 731 -14.879 14.946 35.299 1.00 15.21 C ANISOU 3294 CD 1 LEU A 731 2503 1992 1283 267 383 291 C

ATOM 3295 CD2 LEU A 731 -17.072 15.360 34.166 1.00 23.58 C ANISOU 3295 CD2 LEU A 731 3459 3029 2471 269 452 262 C

ATOM 3296 C LEU A 731 -15.549 11.432 35.322 1.00 16.61 C

ANISOU 3296 C LEU A 731 2586 2131 1594 275 489 335 C

ATOM 3297 O LEU A 731 -15.278 11.778 36.466 1.00 17.31 O

ANISOU 3297 O LEU A 731 2762 2208 1608 295 504 354 O

ATOM 3298 N LYS A 732 -16.446 10.487 35.068 1.00 16.45 N

ANISOU 3298 N LYS A 732 2508 2088 1657 278 550 338 N

ATOM 3299 CA LYS A 732 -17.128 9.832 36.182 1.00 14.13 C

ANISOU 3299 CA LYS A 732 2254 1748 1367 304 643 367 C

ATOM 3300 CB LYS A 732 -18.179 8.860 35.679 1.00 10.38 C

ANISOU 3300 CB LYS A 732 1697 1248 1001 302 707 361 C

ATOM 3301 CG LYS A 732 -18.982 8.211 36.797 1.00 20.84 C

ANISOU 3301 CG LYS A 732 3060 2519 2339 330 813 389 C

ATOM 3302 CD LYS A 732 -19.986 7.219 36.235 1.00 46.75 C

ANISOU 3302 CD LYS A 732 6252 5774 5737 324 876 379 C

ATOM 3303 CE LYS A 732 -20.724 6.486 37.343 1.00 69.38 C

ANISOU 3303 CE LYS A 732 9156 8584 8621 351 988 409 C

ATOM 3304 NZ LYS A 732 -21.702 5.502 36.795 1.00 80.95 N

ANISOU 3304 NZ LYS A 732 10529 10020 10207 344 1052 395 N

ATOM 3305 C LYS A 732 -16.142 9.106 37.095 1.00 17.08 C

ANISOU 3305 C LYS A 732 2694 2121 1675 318 638 401 C

ATOM 3306 O LYS A 732 -16.232 9.201 38.321 1.00 15.52 O

ANISOU 3306 O LYS A 732 2580 1898 1420 346 684 426 O

ATOM 3307 N ALA A 733 -15.230 8.356 36.477 1.00 15.72 N

ANISOU 3307 N ALA A 733 2484 1976 1514 300 584 401 N

ATOM 3308 CA ALA A 733 -14.181 7.624 37.182 1.00 15.47 C

ANISOU 3308 CA ALA A 733 2505 1949 1424 311 567 430 C

ATOM 3309 CB ALA A 733 -13.339 6.831 36.187 1.00 14.42 C

ANISOU 3309 CB ALA A 733 2305 1846 1326 284 507 423 C

ATOM 3310 C ALA A 733 -13.295 8.553 38.014 1.00 16.26 C

ANISOU 3310 C ALA A 733 2700 2066 1414 324 518 436 C

ATOM 3311 O ALA A 733 -12.918 8.226 39.138 1.00 20.08 O

ANISOU 3311 O ALA A 733 3260 2535 1834 351 540 464 O

ATOM 3312 N PHE A 734 -12.954 9.705 37.446 1.00 14.20 N

ANISOU 3312 N PHE A 734 2431 1833 1130 305 452 406 N

ATOM 3313 CA PHE A 734 -12.197 10.715 38.162 1.00 15.28 C

ANISOU 3313 CA PHE A 734 2641 1978 1188 316 401 394 C

ATOM 3314 CB PHE A 734 -11.867 11.886 37.235 1.00 14.48 C ANISOU 3314 CB PHE A 734 2502 1903 1097 289 328 353 C

ATOM 3315 CG PHE A 734 -11.215 13.045 37.934 1.00 14.71 C

ANISOU 3315 CG PHE A 734 2595 1930 1064 297 283 332 C

ATOM 3316 CD1 PHE A 734 -11.822 14.296 37.942 1.00 16.50 C

ANISOU 3316 CD 1 PHE A 734 2839 2150 1281 297 292 315 C

ATOM 3317 CD2 PHE A 734 -10.015 12.881 38.604 1.00 19.86 C

ANISOU 3317 CD2 PHE A 734 3290 2588 1669 305 234 329 C

ATOM 3318 CE1 PHE A 734 -11.226 15.367 38.588 1.00 21.52 C

ANISOU 3318 CE1 PHE A 734 3532 2782 1862 304 254 295 C

ATOM 3319 CE2 PHE A 734 -9.420 13.950 39.263 1.00 21.49 C

ANISOU 3319 CE2 PHE A 734 3554 2792 1821 312 196 309 C

ATOM 3320 CZ PHE A 734 -10.032 15.194 39.249 1.00 14.62 C

ANISOU 3320 CZ PHE A 734 2698 1913 943 310 206 292 C

ATOM 3321 C PHE A 734 -12.953 11.209 39.405 1.00 10.36 C

ANISOU 3321 C PHE A 734 2098 1320 517 349 470 411 C

ATOM 3322 O PHE A 734 -12.436 11.143 40.519 1.00 13.49 O

ANISOU 3322 O PHE A 734 2571 1705 851 376 470 424 O

ATOM 3323 N LEU A 735 -14.180 11.678 39.201 1.00 15.49 N

ANISOU 3323 N LEU A 735 2731 1953 1201 348 530 408 N

ATOM 3324 CA LEU A 735 -15.022 12.118 40.301 1.00 20.31 C

ANISOU 3324 CA LEU A 735 3410 2527 1781 378 605 423 C

ATOM 3325 CB LEU A 735 -16.409 12.524 39.783 1.00 22.25 C

ANISOU 3325 CB LEU A 735 3601 2749 2103 373 661 406 C

ATOM 3326 CG LEU A 735 -16.459 13.668 38.754 1.00 23.57 C

ANISOU 3326 CG LEU A 735 3722 2945 2289 348 603 369 C

ATOM 3327 CD1 LEU A 735 -17.850 13.806 38.135 1.00 18.09 C

ANISOU 3327 CD 1 LEU A 735 2960 2229 1684 345 658 353 C

ATOM 3328 CD2 LEU A 735 -15.996 15.012 39.350 1.00 18.02 C

ANISOU 3328 CD2 LEU A 735 3097 2252 1498 354 567 360 C

ATOM 3329 C LEU A 735 -15.128 11.027 41.371 1.00 24.23 C

ANISOU 3329 C LEU A 735 3958 2991 2259 410 673 462 C

ATOM 3330 O LEU A 735 -15.070 11.316 42.564 1.00 13.17 O

ANISOU 3330 O LEU A 735 2648 1573 785 441 700 479 O

ATOM 3331 N ASP A 736 -15.241 9.770 40.946 1.00 18.42 N

ANISOU 3331 N ASP A 736 3163 2246 1588 405 699 475 N

ATOM 3332 CA ASP A 736 -15.354 8.667 41.898 1.00 27.74 C

ANISOU 3332 CA ASP A 736 4389 3394 2758 436 769 514 C

ATOM 3333 CB ASP A 736 -15.715 7.359 41.187 1.00 31.11 C

ANISOU 3333 CB ASP A 736 4730 3807 3283 422 806 520 C

ATOM 3334 CG ASP A 736 -17.166 7.318 40.762 1.00 30.58 C

ANISOU 3334 CG ASP A 736 4598 3707 3314 417 883 507 C

ATOM 3335 OD1 ASP A 736 -17.926 8.183 41.231 1.00 31.28 O

ANISOU 3335 OD1 ASP A 736 4722 3774 3388 430 922 501 O

ATOM 3336 OD2 ASP A 736 -17.549 6.433 39.969 1.00 37.28 O

ANISOU 3336 OD2 ASP A 736 5361 4549 4254 400 904 499 O

ATOM 3337 C ASP A 736 -14.105 8.481 42.758 1.00 27.13 C ANISOU 3337 C ASP A 736 4395 3333 2579 457 723 535 C

ATOM 3338 O ASP A 736 -14.158 7.886 43.820 1.00 24.37 O

ANISOU 3338 O ASP A 736 4113 2956 2190 493 780 569 O

ATOM 3339 N SER A 737 -12.975 8.979 42.292 1.00 12.81 N

ANISOU 3339 N SER A 737 2569 1560 740 438 616 506 N

ATOM 3340 CA SER A 737 -11.749 8.855 43.063 1.00 25.92 C

ANISOU 3340 CA SER A 737 4289 3231 2327 460 559 508 C

ATOM 3341 CB SER A 737 -10.537 8.881 42.136 1.00 24.67 C

ANISOU 3341 CB SER A 737 4074 3115 2184 427 452 477 C

ATOM 3342 OG SER A 737 -10.283 10.202 41.683 1.00 21.96 O

ANISOU 3342 OG SER A 737 3719 2792 1835 404 388 436 O

ATOM 3343 C SER A 737 -11.656 10.003 44.054 1.00 29.70 C

ANISOU 3343 C SER A 737 4854 3701 2729 484 547 496 C

ATOM 3344 O SER A 737 -10.722 10.070 44.846 1.00 29.28 O

ANISOU 3344 O SER A 737 4862 3654 2607 507 503 494 O

ATOM 3345 N LEU A 738 -12.638 10.900 44.001 1.00 27.32 N

ANISOU 3345 N LEU A 738 4554 3385 2439 480 587 486 N

ATOM 3346 CA LEU A 738 -12.658 12.082 44.846 1.00 30.44 C

ANISOU 3346 CA LEU A 738 5026 3772 2769 499 579 472 C

ATOM 3347 CB LEU A 738 -13.063 13.304 44.027 1.00 21.45 C

ANISOU 3347 CB LEU A 738 3843 2645 1661 467 552 436 C

ATOM 3348 CG LEU A 738 -12.116 13.689 42.890 1.00 26.36 C

ANISOU 3348 CG LEU A 738 4397 3307 2312 428 450 399 C ATOM 3349 CD1 LEU A 738 -12.612 14.968 42.214 1.00 21.49 C ANISOU 3349 CD1 LEU A 738 3750 2697 1720 405 434 368 C ATOM 3350 CD2 LEU A 738 -10.707 13.854 43.410 1.00 30.37 C ANISOU 3350 CD2 LEU A 738 4946 3831 2761 434 370 384 C

ATOM 3351 C LEU A 738 -13.604 11.939 46.038 1.00 29.53 C

ANISOU 3351 C LEU A 738 4989 3613 2619 540 682 506 C

ATOM 3352 O LEU A 738 -14.742 11.497 45.891 1.00 41.16 O

ANISOU 3352 O LEU A 738 6436 5058 4144 541 772 527 O

ATOM 3353 N PRO A 739 -13.133 12.339 47.216 1.00 26.87 N

ANISOU 3353 N PRO A 739 4747 3267 2195 576 671 509 N

ATOM 3354 CD PRO A 739 -11.763 12.837 47.419 1.00 34.28 C

ANISOU 3354 CD PRO A 739 5712 4237 3077 575 567 480 C

ATOM 3355 CA PRO A 739 -13.895 12.280 48.471 1.00 37.00 C

ANISOU 3355 CA PRO A 739 6120 4508 3431 621 763 541 C

ATOM 3356 CB PRO A 739 -12.912 12.840 49.512 1.00 46.30 C

ANISOU 3356 CB PRO A 739 7388 5695 4507 651 705 529 C

ATOM 3357 CG PRO A 739 -11.867 13.568 48.723 1.00 45.69 C

ANISOU 3357 CG PRO A 739 7263 5661 4437 614 589 483 C

ATOM 3358 C PRO A 739 -15.203 13.082 48.490 1.00 44.24 C

ANISOU 3358 C PRO A 739 7038 5397 4373 617 836 538 C

ATOM 3359 O PRO A 739 -16.270 12.474 48.537 1.00 71.19 O

ANISOU 3359 O PRO A 739 10439 8778 7834 625 935 566 O

ATOM 3360 N ASP A 740 -15.128 14.410 48.458 1.00 40.33 N ANISOU 3360 N ASP A 740 6557 4913 3852 606 791 504 N

ATOM 3361 CA ASP A 740 -16.272 15.244 48.853 1.00 48.18 C

ANISOU 3361 CA ASP A 740 7584 5878 4846 615 863 505 C

ATOM 3362 CB ASP A 740 -15.806 16.365 49.788 1.00 53.48 C

ANISOU 3362 CB ASP A 740 8343 6548 5428 636 826 486 C

ATOM 3363 CG ASP A 740 -15.062 15.843 51.004 1.00 64.01 C

ANISOU 3363 CG ASP A 740 9769 7875 6675 681 820 507 C

ATOM 3364 OD1 ASP A 740 -15.545 14.872 51.627 1.00 73.09 O ANISOU 3364 OD1 ASP A 740 10955 8995 7820 714 902 548 O

ATOM 3365 OD2 ASP A 740 -13.996 16.406 51.338 1.00 57.42 O ANISOU 3365 OD2 ASP A 740 8972 7065 5780 685 735 482 O

ATOM 3366 C ASP A 740 -17.090 15.849 47.705 1.00 44.67 C

ANISOU 3366 C ASP A 740 7054 5440 4481 576 871 482 C

ATOM 3367 O ASP A 740 -17.485 17.016 47.768 1.00 35.17 O

ANISOU 3367 O ASP A 740 5867 4232 3264 572 870 462 O

ATOM 3368 N VAL A 741 -17.352 15.050 46.677 1.00 27.01 N

ANISOU 3368 N VAL A 741 4726 3212 2323 550 880 487 N

ATOM 3369 CA VAL A 741 -18.139 15.484 45.524 1.00 30.67 C ANISOU 3369 CA VAL A 741 5103 3685 2864 517 889 466 C

ATOM 3370 CB VAL A 741 -17.909 14.543 44.316 1.00 27.74 C

ANISOU 3370 CB VAL A 741 4630 3336 2574 487 857 461 C

ATOM 3371 CGI VAL A 741 -18.896 14.847 43.187 1.00 25.90 C ANISOU 3371 CGI VAL A 741 4301 3099 2442 462 873 435 C

ATOM 3372 CG2 VAL A 741 -16.460 14.648 43.831 1.00 24.01 C ANISOU 3372 CG2 VAL A 741 4146 2910 2067 468 741 442 C

ATOM 3373 C VAL A 741 -19.641 15.563 45.827 1.00 30.84 C

ANISOU 3373 C VAL A 741 5120 3657 2940 531 997 475 C

ATOM 3374 O VAL A 741 -20.237 14.606 46.316 1.00 35.72 O

ANISOU 3374 O VAL A 741 5745 4236 3590 552 1079 503 O

ATOM 3375 N LYS A 742 -20.248 16.708 45.526 1.00 26.14 N

ANISOU 3375 N LYS A 742 4512 3060 2359 521 997 450 N

ATOM 3376 CA LYS A 742 -21.694 16.871 45.676 1.00 32.73 C

ANISOU 3376 CA LYS A 742 5330 3850 3257 531 1092 452 C

ATOM 3377 CB LYS A 742 -22.020 18.145 46.465 1.00 41.35 C

ANISOU 3377 CB LYS A 742 6500 4927 4286 548 1112 446 C

ATOM 3378 CG LYS A 742 -21.660 18.033 47.943 1.00 70.06 C

ANISOU 3378 CG LYS A 742 10254 8542 7822 586 1146 475 C

ATOM 3379 CD LYS A 742 -22.258 19.155 48.777 1.00 76.61 C

ANISOU 3379 CD LYS A 742 11158 9346 8605 605 1190 472 C

ATOM 3380 CE LYS A 742 -22.027 18.907 50.261 1.00 78.47 C

ANISOU 3380 CE LYS A 742 11511 9556 8747 649 1235 503 C

ATOM 3381 NZ LYS A 742 -22.621 19.975 51.114 1.00 83.52 N

ANISOU 3381 NZ LYS A 742 12225 10168 9339 669 1281 500 N

ATOM 3382 C LYS A 742 -22.418 16.860 44.331 1.00 30.54 C

ANISOU 3382 C LYS A 742 4935 3579 3090 502 1088 425 C

ATOM 3383 O LYS A 742 -21.921 17.385 43.339 1.00 29.63 O ANISOU 3383 O LYS A 742 4770 3505 2984 475 1006 398 O

ATOM 3384 N ILE A 743 -23.599 16.256 44.305 1.00 26.85 N

ANISOU 3384 N ILE A 743 4425 3070 2708 510 1177 432 N

ATOM 3385 CA ILE A 743 -24.358 16.100 43.073 1.00 29.84 C

ANISOU 3385 CA ILE A 743 4688 3452 3198 487 1178 405 C

ATOM 3386 CB ILE A 743 -24.805 14.633 42.894 1.00 23.86 C

ANISOU 3386 CB ILE A 743 3872 2669 2524 488 1236 419 C

ATOM 3387 CG2 ILE A 743 -25.625 14.473 41.625 1.00 34.02 C

ANISOU 3387 CG2 ILE A 743 5038 3959 3927 466 1236 386 C

ATOM 3388 CGI ILE A 743 -23.595 13.698 42.870 1.00 35.09 C

ANISOU 3388 CGI ILE A 743 5304 4118 3910 483 1185 436 C

ATOM 3389 CD 1 ILE A 743 -22.815 13.724 41.561 1.00 21.02 C

ANISOU 3389 CD 1 ILE A 743 3448 2391 2149 449 1082 409 C

ATOM 3390 C ILE A 743 -25.598 16.990 43.037 1.00 41.35 C

ANISOU 3390 C ILE A 743 6130 4882 4698 492 1230 388 C

ATOM 3391 O ILE A 743 -26.622 16.672 43.645 1.00 40.55 O

ANISOU 3391 O ILE A 743 6037 4730 4638 512 1328 401 O

ATOM 3392 N VAL A 744 -25.511 18.106 42.321 1.00 23.89 N

ANISOU 3392 N VAL A 744 3895 2702 2481 476 1168 359 N

ATOM 3393 CA VAL A 744 -26.650 18.996 42.198 1.00 34.73 C

ANISOU 3393 CA VAL A 744 5248 4052 3895 481 1210 341 C

ATOM 3394 CB VAL A 744 -26.190 20.404 41.804 1.00 38.94 C

ANISOU 3394 CB VAL A 744 5800 4620 4375 470 1136 318 C

ATOM 3395 CGI VAL A 744 -27.383 21.267 41.420 1.00 40.60 C ANISOU 3395 CGI VAL A 744 5971 4813 4642 473 1171 296 C

ATOM 3396 CG2 VAL A 744 -25.403 21.024 42.944 1.00 32.72 C ANISOU 3396 CG2 VAL A 744 5128 3834 3471 483 1123 335 C

ATOM 3397 C VAL A 744 -27.628 18.460 41.163 1.00 37.01 C

ANISOU 3397 C VAL A 744 5422 4334 4308 470 1235 319 C

ATOM 3398 O VAL A 744 -27.240 18.169 40.034 1.00 38.66 O

ANISOU 3398 O VAL A 744 5556 4579 4554 449 1169 299 O

ATOM 3399 N LYS A 745 -28.891 18.313 41.551 1.00 50.12 N

ANISOU 3399 N LYS A 745 6918 6868 5256 -104 879 319 N

ATOM 3400 CA LYS A 745 -29.918 17.791 40.648 1.00 53.59 C

ANISOU 3400 CA LYS A 745 7282 7313 5766 -148 926 429 C

ATOM 3401 CB LYS A 745 -31.139 17.277 41.428 1.00 57.76 C

ANISOU 3401 CB LYS A 745 7836 7903 6207 -164 1025 496 C

ATOM 3402 CG LYS A 745 -31.010 15.855 41.982 1.00 53.40 C

ANISOU 3402 CG LYS A 745 7374 7381 5533 -197 982 567 C

ATOM 3403 CD LYS A 745 -32.349 15.345 42.536 1.00 49.65 C

ANISOU 3403 CD LYS A 745 6904 6970 4993 -222 1084 652 C

ATOM 3404 CE LYS A 745 -32.244 13.913 43.071 1.00 51.10 C

ANISOU 3404 CE LYS A 745 7173 7182 5061 -261 1035 732 C

ATOM 3405 NZ LYS A 745 -33.580 13.311 43.426 1.00 42.67 N

ANISOU 3405 NZ LYS A 745 6098 6173 3941 -294 1127 834 N

ATOM 3406 C LYS A 745 -30.353 18.843 39.632 1.00 67.36 C ANISOU 3406 C LYS A 745 8907 9024 7663 -143 966 418 C

ATOM 3407 O LYS A 745 -30.518 20.015 39.974 1.00 76.59 O ANISOU 3407 O LYS A 745 10048 10188 8866 -103 1017 343 O

ATOM 3408 N MET A 746 -30.537 18.412 38.385 1.00 71.31 N

ANISOU 3408 N MET A 746 9335 9501 8257 -186 939 494 N ATOM 3409 CA MET A 746 -30.946 19.305 37.303 1.00 78.11 C ANISOU 3409 CA MET A 746 10077 10333 9268 -193 968 500 C ATOM 3410 CB MET A 746 -30.133 19.029 36.028 1.00 78.91 C ANISOU 3410 CB MET A 746 10133 10396 9453 -225 868 518 C ATOM 3411 CG MET A 746 -28.625 19.271 36.150 1.00 79.64 C ANISOU 3411 CG MET A 746 10273 10458 9527 -197 762 425 C

ATOM 3412 SD MET A 746 -27.765 19.310 34.548 1.00 31.05 S ANISOU 3412 SD MET A 746 4036 4264 3497 -231 663 432 S

ATOM 3413 CE MET A 746 -28.604 20.699 33.778 1.00 37.99 C ANISOU 3413 CE MET A 746 4782 5127 4524 -232 735 437 C

ATOM 3414 C MET A 746 -32.439 19.168 37.006 1.00 75.90 C ANISOU 3414 C MET A 746 9731 10080 9029 -223 1071 594 C

ATOM 3415 O MET A 746 -33.287 19.603 37.788 1.00 73.42 O ANISOU 3415 O MET A 746 9418 9794 8682 -199 1168 584 O

ATOM 3416 N LEU A 762 -29.632 15.212 33.236 1.00 30.06 N

ANISOU 3416 N LEU A 762 3918 4191 3313 -386 662 747 N

ATOM 3417 CA LEU A 762 -29.033 14.331 34.236 1.00 55.81 C

ANISOU 3417 CA LEU A 762 7298 7463 6443 -377 625 741 C

ATOM 3418 CB LEU A 762 -27.755 13.686 33.685 1.00 62.51 C

ANISOU 3418 CB LEU A 762 8168 8282 7300 -386 504 711 C

ATOM 3419 CG LEU A 762 -27.269 12.398 34.359 1.00 53.75 C

ANISOU 3419 CG LEU A 762 7160 7174 6089 -391 440 730 C ATOM 3420 CD1 LEU A 762 -28.149 11.228 33.964 1.00 44.29 C ANISOU 3420 CD 1 LEU A 762 5935 5980 4912 -432 440 814 C ATOM 3421 CD2 LEU A 762 -25.819 12.109 34.008 1.00 56.14 C ANISOU 3421 CD2 LEU A 762 7485 7442 6403 -382 321 667 C

ATOM 3422 C LEU A 762 -28.724 15.080 35.535 1.00 57.12 C

ANISOU 3422 C LEU A 762 7532 7639 6531 -320 649 658 C

ATOM 3423 O LEU A 762 -29.605 15.686 36.146 1.00 64.66 O

ANISOU 3423 O LEU A 762 8479 8619 7470 -302 744 660 O

ATOM 3424 N ASN A 763 -27.467 15.022 35.960 1.00 58.57 N

ANISOU 3424 N ASN A 763 7782 7804 6667 -293 562 584 N

ATOM 3425 CA ASN A 763 -27.026 15.740 37.149 1.00 46.13 C ANISOU 3425 CA ASN A 763 6274 6236 5018 -241 571 497 C

ATOM 3426 CB ASN A 763 -27.001 14.821 38.384 1.00 51.70 C

ANISOU 3426 CB ASN A 763 7093 6971 5580 -238 563 516 C

ATOM 3427 CG ASN A 763 -26.076 13.621 38.219 1.00 49.64 C ANISOU 3427 CG ASN A 763 6886 6689 5285 -259 452 537 C ATOM 3428 OD1 ASN A 763 -24.862 13.716 38.428 1.00 35.84 O ANISOU 3428 OD1 ASN A 763 5183 4917 3519 -235 365 466 O ATOM 3429 ND2 ASN A 763 -26.651 12.477 37.865 1.00 58.63 N ANISOU 3429 ND2 ASN A 763 8023 7837 6419 -304 451 634 N

ATOM 3430 C ASN A 763 -25.674 16.423 36.946 1.00 34.68 C

ANISOU 3430 C ASN A 763 4825 4748 3602 -210 484 398 C

ATOM 3431 O ASN A 763 -24.882 16.040 36.074 1.00 26.08 O

ANISOU 3431 O ASN A 763 3712 3632 2565 -228 399 398 O

ATOM 3432 N MET A 764 -25.416 17.448 37.747 1.00 26.38 N

ANISOU 3432 N MET A 764 3800 3698 2526 -162 506 313 N

ATOM 3433 CA MET A 764 -24.139 18.145 37.676 1.00 22.75 C

ANISOU 3433 CA MET A 764 3348 3204 2093 -131 424 218 C

ATOM 3434 CB MET A 764 -24.351 19.642 37.422 1.00 27.02 C

ANISOU 3434 CB MET A 764 3813 3728 2726 -103 470 160 C

ATOM 3435 CG MET A 764 -23.059 20.416 37.244 1.00 25.17 C

ANISOU 3435 CG MET A 764 3574 3456 2532 -74 383 68 C

ATOM 3436 SD MET A 764 -23.278 22.198 37.038 1.00 24.19 S

ANISOU 3436 SD MET A 764 3364 3307 2519 -40 429 -3 S

ATOM 3437 CE MET A 764 -23.721 22.717 38.688 1.00 18.10 C

ANISOU 3437 CE MET A 764 2677 2561 1640 11 507 -69 C

ATOM 3438 C MET A 764 -23.333 17.940 38.948 1.00 24.39 C

ANISOU 3438 C MET A 764 3673 3418 2177 -98 378 158 C

ATOM 3439 O MET A 764 -23.646 18.516 39.998 1.00 26.93 O

ANISOU 3439 O MET A 764 4038 3762 2433 -66 436 113 O

ATOM 3440 N PRO A 765 -22.281 17.117 38.866 1.00 16.79 N

ANISOU 3440 N PRO A 765 2760 2437 1183 -107 274 154 N

ATOM 3441 CD PRO A 765 -21.857 16.318 37.712 1.00 12.15 C

ANISOU 3441 CD PRO A 765 2130 1827 661 -144 203 200 C

ATOM 3442 CA PRO A 765 -21.375 16.946 40.007 1.00 24.44 C

ANISOU 3442 CA PRO A 765 3837 3407 2043 -79 215 96 C

ATOM 3443 CB PRO A 765 -20.435 15.820 39.547 1.00 17.25 C

ANISOU 3443 CB PRO A 765 2953 2471 1130 -102 104 122 C

ATOM 3444 CG PRO A 765 -21.109 15.206 38.358 1.00 17.59 C

ANISOU 3444 CG PRO A 765 2915 2512 1255 -147 123 207 C

ATOM 3445 C PRO A 765 -20.571 18.211 40.269 1.00 18.60 C

ANISOU 3445 C PRO A 765 3097 2645 1326 -33 189 -13 C

ATOM 3446 O PRO A 765 -20.157 18.891 39.341 1.00 16.46 O

ANISOU 3446 O PRO A 765 2750 2343 1163 -29 159 -44 O

ATOM 3447 N VAL A 766 -20.347 18.512 41.539 1.00 17.01 N

ANISOU 3447 N VAL A 766 2980 2460 1022 -2 198 -70 N

ATOM 3448 CA VAL A 766 -19.627 19.709 41.939 1.00 24.48 C

ANISOU 3448 CA VAL A 766 3936 3386 1980 43 176 -177 C

ATOM 3449 CB VAL A 766 -20.541 20.661 42.734 1.00 28.08 C

ANISOU 3449 CB VAL A 766 4391 3870 2407 71 285 -218 C

ATOM 3450 CGI VAL A 766 -19.753 21.858 43.221 1.00 24.85 C

ANISOU 3450 CGI VAL A 766 4001 3438 2005 118 256 -334 C

ATOM 3451 CG2 VAL A 766 -21.734 21.104 41.887 1.00 19.77 C

ANISOU 3451 CG2 VAL A 766 3230 2820 1461 57 378 -171 C

ATOM 3452 C VAL A 766 -18.448 19.316 42.823 1.00 28.00 C ANISOU 3452 C VAL A 766 4487 3825 2324 59 83 -224 C

ATOM 3453 O VAL A 766 -18.626 18.633 43.831 1.00 28.53 O

ANISOU 3453 O VAL A 766 4642 3928 2271 52 93 -202 O

ATOM 3454 N ILE A 767 -17.244 19.730 42.441 1.00 21.11 N

ANISOU 3454 N ILE A 767 3606 2912 1502 76 -10 -285 N

ATOM 3455 CA ILE A 767 -16.053 19.459 43.250 1.00 21.21 C

ANISOU 3455 CA ILE A 767 3715 2914 1430 93 -104 -334 C

ATOM 3456 CB ILE A 767 -14.830 19.204 42.357 1.00 31.51 C

ANISOU 3456 CB ILE A 767 4991 4175 2808 88 -220 -346 C

ATOM 3457 CG2 ILE A 767 -13.582 19.018 43.200 1.00 39.16 C

ANISOU 3457 CG2 ILE A 767 6053 5128 3697 108 -318 -400 C

ATOM 3458 CGI ILE A 767 -15.067 17.996 41.450 1.00 30.39 C

ANISOU 3458 CGI ILE A 767 4812 4031 2704 45 -240 -255 C

ATOM 3459 CD1 ILE A 767 -14.051 17.863 40.335 1.00 31.73 C

ANISOU 3459 CD 1 ILE A 767 4925 4162 2968 37 -335 -268 C

ATOM 3460 C ILE A 767 -15.755 20.661 44.141 1.00 21.82 C

ANISOU 3460 C ILE A 767 3828 2991 1471 137 -89 -436 C

ATOM 3461 O ILE A 767 -15.701 21.788 43.660 1.00 26.80 O

ANISOU 3461 O ILE A 767 4392 3598 2195 159 -75 -489 O

ATOM 3462 N PRO A 768 -15.582 20.431 45.455 1.00 34.86 N

ANISOU 3462 N PRO A 768 5585 4671 2988 147 -93 -461 N

ATOM 3463 CD PRO A 768 -15.614 19.115 46.113 1.00 42.65 C

ANISOU 3463 CD PRO A 768 6655 5689 3862 118 -117 -394 C

ATOM 3464 CA PRO A 768 -15.366 21.527 46.415 1.00 40.01 C

ANISOU 3464 CA PRO A 768 6280 5330 3591 187 -73 -561 C

ATOM 3465 CB PRO A 768 -15.436 20.821 47.774 1.00 50.57 C

ANISOU 3465 CB PRO A 768 7734 6717 4765 178 -67 -549 C

ATOM 3466 CG PRO A 768 -15.064 19.405 47.484 1.00 50.98 C

ANISOU 3466 CG PRO A 768 7814 6764 4793 140 -141 -462 C

ATOM 3467 C PRO A 768 -14.013 22.222 46.255 1.00 37.93 C

ANISOU 3467 C PRO A 768 6020 5018 3374 215 -174 -644 C

ATOM 3468 O PRO A 768 -13.057 21.614 45.770 1.00 29.52 O

ANISOU 3468 O PRO A 768 4960 3923 2332 203 -275 -624 O

ATOM 3469 N MET A 769 -13.942 23.483 46.679 1.00 53.52 N

ANISOU 3469 N MET A 769 7990 6982 5362 253 -148 -736 N

ATOM 3470 CA MET A 769 -12.731 24.299 46.545 1.00 57.28 C

ANISOU 3470 CA MET A 769 8463 7411 5888 281 -238 -818 C

ATOM 3471 CB MET A 769 -13.059 25.783 46.753 1.00 49.72 C

ANISOU 3471 CB MET A 769 7467 6441 4982 320 -181 -906 C

ATOM 3472 CG MET A 769 -11.878 26.730 46.590 1.00 50.17 C

ANISOU 3472 CG MET A 769 7514 6447 5101 349 -271 -991 C

ATOM 3473 SD MET A 769 -11.056 26.611 44.991 1.00 64.93 S

ANISOU 3473 SD MET A 769 9287 8268 7117 329 -366 -949 S

ATOM 3474 CE MET A 769 -9.705 27.768 45.224 1.00 69.92 C

ANISOU 3474 CE MET A 769 9933 8851 7783 367 -464 -1058 C

ATOM 3475 C MET A 769 -11.602 23.866 47.488 1.00 54.43 C ANISOU 3475 C MET A 769 8214 7051 5416 287 -333 -852 C

ATOM 3476 O MET A 769 -11.095 24.657 48.290 1.00 49.27 O

ANISOU 3476 O MET A 769 7611 6392 4719 317 -352 -939 O

ATOM 3477 N ASN A 770 -11.199 22.608 47.378 1.00 39.27 N

ANISOU 3477 N ASN A 770 6330 5134 3455 257 -395 -783 N

ATOM 3478 CA ASN A 770 -10.118 22.108 48.201 1.00 29.24 C

ANISOU 3478 CA ASN A 770 5160 3860 2089 257 -492 -803 C

ATOM 3479 CB ASN A 770 -10.545 20.851 48.957 1.00 43.77 C

ANISOU 3479 CB ASN A 770 7078 5745 3805 224 -479 -729 C

ATOM 3480 CG ASN A 770 -11.671 21.125 49.936 1.00 50.59 C

ANISOU 3480 CG ASN A 770 7980 6670 4572 225 -364 -737 C

ATOM 3481 OD1 ASN A 770 -12.520 21.981 49.690 1.00 46.75 O

ANISOU 3481 OD1 ASN A 770 7432 6191 4138 242 -270 -765 O

ATOM 3482 ND2 ASN A 770 -11.683 20.404 51.050 1.00 55.28 N

ANISOU 3482 ND2 ASN A 770 8673 7307 5023 206 -373 -712 N

ATOM 3483 C ASN A 770 -8.820 21.893 47.427 1.00 27.63 C

ANISOU 3483 C ASN A 770 4933 3605 1961 258 -616 -809 C

ATOM 3484 0 ASN A 770 -8.574 22.566 46.423 1.00 29.88 O

ANISOU 3484 O ASN A 770 5129 3855 2368 268 -630 -832 O

ATOM 3485 N THR A 771 -7.985 20.985 47.934 1.00 45.14 N

ANISOU 3485 N THR A 771 7228 5818 4104 245 -705 -789 N

ATOM 3486 CA THR A 771 -6.641 20.744 47.408 1.00 50.90 C

ANISOU 3486 CA THR A 771 7950 6501 4889 248 -830 -802 C

ATOM 3487 CB THR A 771 -5.966 19.564 48.126 1.00 48.31 C

ANISOU 3487 CB THR A 771 7711 6171 4476 230 -910 -759 C

ATOM 3488 OG1 THR A 771 -6.150 19.687 49.541 1.00 48.10 O

ANISOU 3488 OG1 THR A 771 7790 6185 4300 232 -890 -788 O

ATOM 3489 CG2 THR A 771 -4.483 19.532 47.810 1.00 53.09 C ANISOU 3489 CG2 THR A 771 8292 6706 5175 249 -1020 -767 C

ATOM 3490 C THR A 771 -6.632 20.450 45.912 1.00 56.89 C

ANISOU 3490 C THR A 771 8602 7234 5780 233 -844 -759 C

ATOM 3491 O THR A 771 -5.929 21.107 45.139 1.00 48.54 O

ANISOU 3491 O THR A 771 7468 6134 4843 252 -883 -785 O

ATOM 3492 N ILE A 772 -7.400 19.446 45.509 1.00 58.19 N

ANISOU 3492 N ILE A 772 8746 7418 5946 201 -805 -674 N

ATOM 3493 CA ILE A 772 -7.524 19.108 44.099 1.00 44.41 C

ANISOU 3493 CA ILE A 772 6899 5655 4318 182 -809 -630 C

ATOM 3494 CB ILE A 772 -8.501 17.926 43.891 1.00 51.90 C

ANISOU 3494 CB ILE A 772 7845 6630 5247 145 -758 -534 C

ATOM 3495 CG2 ILE A 772 -9.217 18.035 42.554 1.00 49.48 C

ANISOU 3495 CG2 ILE A 772 7422 6323 5054 126 -703 -496 C

ATOM 3496 CGI ILE A 772 -7.746 16.597 43.952 1.00 53.97 C

ANISOU 3496 CGI ILE A 772 8154 6874 5479 126 -855 -492 C

ATOM 3497 CD 1 ILE A 772 -7.081 16.312 45.279 1.00 40.51 C

ANISOU 3497 CD 1 ILE A 772 6562 5167 3662 136 -914 -510 C

ATOM 3498 C ILE A 772 -7.940 20.333 43.260 1.00 46.87 C ANISOU 3498 C ILE A 772 7110 5962 4738 195 -751 -664 C ATOM 3499 O ILE A 772 -7.415 20.553 42.166 1.00 48.38 O

ANISOU 3499 O ILE A 772 7220 6128 5033 191 -795 -672 O

ATOM 3500 N ALA A 773 -8.858 21.144 43.779 1.00 38.52 N

ANISOU 3500 N ALA A 773 6054 4926 3655 209 -655 -686 N

ATOM 3501 CA ALA A 773 -9.326 22.325 43.047 1.00 31.87 C ANISOU 3501 CA ALA A 773 5115 4075 2919 220 -599 -715 C

ATOM 3502 CB ALA A 773 -10.599 22.866 43.652 1.00 23.83 C ANISOU 3502 CB ALA A 773 4102 3088 1865 229 -478 -718 C

ATOM 3503 C ALA A 773 -8.281 23.431 42.964 1.00 35.66 C

ANISOU 3503 C ALA A 773 5578 4519 3451 251 -667 -801 C

ATOM 3504 O ALA A 773 -8.291 24.243 42.045 1.00 25.43 O

ANISOU 3504 O ALA A 773 4188 3205 2270 252 -662 -815 O

ATOM 3505 N GLU A 774 -7.378 23.476 43.931 1.00 44.07 N

ANISOU 3505 N GLU A 774 6734 5575 4436 272 -734 -854 N

ATOM 3506 CA GLU A 774 -6.337 24.488 43.893 1.00 33.64 C ANISOU 3506 CA GLU A 774 5400 4218 3165 301 -805 -931 C

ATOM 3507 CB GLU A 774 -5.664 24.595 45.251 1.00 37.73 C ANISOU 3507 CB GLU A 774 6024 4730 3580 327 -845 -978 C

ATOM 3508 CG GLU A 774 -6.576 25.169 46.322 1.00 37.77 C ANISOU 3508 CG GLU A 774 6092 4771 3489 341 -756 -1029 C

ATOM 3509 CD GLU A 774 -5.896 25.232 47.679 1.00 47.87 C ANISOU 3509 CD GLU A 774 7488 6055 4643 358 -804 -1087 C ATOM 3510 OE1 GLU A 774 -5.424 24.172 48.158 1.00 37.34 O ANISOU 3510 OE1 GLU A 774 6222 4729 3237 342 -856 -1039 O ATOM 3511 OE2 GLU A 774 -5.825 26.344 48.254 1.00 50.69 O ANISOU 3511 OE2 GLU A 774 7862 6405 4991 389 -788 -1170 O

ATOM 3512 C GLU A 774 -5.322 24.141 42.816 1.00 33.59 C

ANISOU 3512 C GLU A 774 5311 4172 3279 296 -884 -882 C

ATOM 3513 O GLU A 774 -4.879 25.006 42.058 1.00 21.74 O

ANISOU 3513 O GLU A 774 3724 2645 1889 308 -907 -900 O

ATOM 3514 N ALA A 775 -4.978 22.859 42.748 1.00 28.75 N

ANISOU 3514 N ALA A 775 4723 3556 2645 278 -922 -819 N

ATOM 3515 CA ALA A 775 -4.015 22.356 41.779 1.00 36.79 C ANISOU 3515 CA ALA A 775 5672 4538 3770 277 -987 -774 C

ATOM 3516 CB ALA A 775 -3.786 20.865 41.982 1.00 29.33 C ANISOU 3516 CB ALA A 775 4779 3588 2779 258 -1020 -717 C

ATOM 3517 C ALA A 775 -4.502 22.639 40.367 1.00 28.40 C

ANISOU 3517 C ALA A 775 4486 3483 2822 255 -950 -745 C

ATOM 3518 O ALA A 775 -3.716 22.990 39.478 1.00 17.33 O

ANISOU 3518 O ALA A 775 3000 2056 1530 265 -988 -739 O

ATOM 3519 N VAL A 776 -5.806 22.505 40.163 1.00 27.31 N

ANISOU 3519 N VAL A 776 4337 3384 2654 225 -873 -727 N

ATOM 3520 CA VAL A 776 -6.385 22.801 38.856 1.00 26.15 C ANISOU 3520 CA VAL A 776 4076 3249 2609 198 -835 -699 C

ATOM 3521 CB VAL A 776 -7.860 22.354 38.749 1.00 29.66 C ANISOU 3521 CB VAL A 776 4526 3739 3004 162 -750 -664 C ATOM 3522 CGI VAL A 776 -8.470 22.891 37.480 1.00 19.86 C ANISOU 3522 CGI VAL A 776 3160 2504 1882 137 -705 -634 C ATOM 3523 CG2 VAL A 776 -7.959 20.832 38.796 1.00 36.89 C ANISOU 3523 CG2 VAL A 776 5485 4666 3865 137 -764 -599 C ATOM 3524 C VAL A 776 -6.250 24.276 38.471 1.00 27.21 C ANISOU 3524 C VAL A 776 4141 3372 2828 215 -832 -750 C ATOM 3525 O VAL A 776 -5.839 24.592 37.353 1.00 21.20 O ANISOU 3525 O VAL A 776 3276 2598 2180 207 -853 -726 O ATOM 3526 N ILE A 777 -6.575 25.187 39.385 1.00 17.94 N ANISOU 3526 N ILE A 777 3020 2197 1598 238 -805 -820 N ATOM 3527 CA ILE A 777 -6.490 26.597 39.045 1.00 20.68 C ANISOU 3527 CA ILE A 777 3301 2525 2031 253 -805 -872 C ATOM 3528 CB ILE A 777 -7.282 27.516 40.010 1.00 25.54 C ANISOU 3528 CB ILE A 777 3960 3141 2605 281 -732 -929 C ATOM 3529 CG2 ILE A 777 -6.723 27.424 41.416 1.00 49.43 C ANISOU 3529 CG2 ILE A 777 7112 6163 5507 313 -763 -988 C ATOM 3530 CGI ILE A 777 -7.246 28.958 39.486 1.00 41.16 C ANISOU 3530 CGI ILE A 777 5850 5090 4700 294 -733 -971 C ATOM 3531 CD1 ILE A 777 -8.171 29.933 40.208 1.00 40.81 C ANISOU 3531 CD 1 ILE A 777 5812 5039 4654 323 -645 -1015 C ATOM 3532 C ILE A 777 -5.052 27.069 38.934 1.00 12.46 C ANISOU 3532 C ILE A 777 2234 1448 1054 285 -894 -885 C ATOM 3533 O ILE A 777 -4.759 28.012 38.205 1.00 21.33 O ANISOU 3533 O ILE A 777 3269 2555 2281 289 -913 -895 O ATOM 3534 N GLU A 778 -4.155 26.397 39.641 1.00 22.16 N ANISOU 3534 N GLU A 778 3537 2661 2220 306 -948 -880 N ATOM 3535 CA GLU A 778 -2.738 26.723 39.550 1.00 29.97 C ANISOU 3535 CA GLU A 778 4508 3614 3265 338 -1031 -889 C ATOM 3536 CB GLU A 778 -1.940 25.965 40.610 1.00 31.47 C ANISOU 3536 CB GLU A 778 4806 3788 3364 358 -1083 -895 C ATOM 3537 CG GLU A 778 -0.438 26.215 40.545 1.00 53.62 C ANISOU 3537 CG GLU A 778 7599 6552 6223 392 -1169 -903 C ATOM 3538 CD GLU A 778 0.348 25.363 41.524 1.00 64.70 C ANISOU 3538 CD GLU A 778 9105 7935 7543 406 -1224 -901 C ATOM 3539 OE1 GLU A 778 -0.236 24.922 42.536 1.00 66.00 O ANISOU 3539 OE1 GLU A 778 9366 8119 7593 397 -1200 -914 O ATOM 3540 OE2 GLU A 778 1.554 25.138 41.280 1.00 67.48 O ANISOU 3540 OE2 GLU A 778 9442 8252 7945 426 -1291 -889 O ATOM 3541 C GLU A 778 -2.222 26.394 38.150 1.00 22.88 C ANISOU 3541 C GLU A 778 3502 2708 2481 324 -1051 -829 C ATOM 3542 O GLU A 778 -1.484 27.175 37.552 1.00 22.55 O ANISOU 3542 O GLU A 778 3392 2647 2530 340 -1086 -837 O ATOM 3543 N MET A 779 -2.608 25.230 37.638 1.00 17.97 N ANISOU 3543 N MET A 779 2871 2104 1854 293 -1026 -770 N ATOM 3544 CA MET A 779 -2.292 24.854 36.266 1.00 20.01 C ANISOU 3544 CA MET A 779 3029 2360 2215 276 -1025 -716 C

ATOM 3545 CB MET A 779 -3.016 23.563 35.875 1.00 16.58 C

ANISOU 3545 CB MET A 779 2597 1948 1755 237 -986 -660 C

ATOM 3546 CG MET A 779 -2.846 23.194 34.402 1.00 12.71 C

ANISOU 3546 CG MET A 779 2004 1461 1366 215 -969 -610 C

ATOM 3547 SD MET A 779 -3.637 21.644 33.927 1.00 21.39 S

ANISOU 3547 SD MET A 779 3106 2581 2441 170 -930 -547 S

ATOM 3548 CE MET A 779 -5.362 22.007 34.189 1.00 16.91 C

ANISOU 3548 CE MET A 779 2544 2060 1820 132 -858 -542 C

ATOM 3549 C MET A 779 -2.697 25.965 35.304 1.00 18.63 C

ANISOU 3549 C MET A 779 2747 2197 2134 262 -995 -717 C

ATOM 3550 O MET A 779 -1.895 26.426 34.496 1.00 20.15 O

ANISOU 3550 O MET A 779 2868 2373 2416 273 -1020 -709 O

ATOM 3551 N ILE A 780 -3.957 26.369 35.386 1.00 21.30 N

ANISOU 3551 N ILE A 780 3078 2563 2453 235 -938 -727 N

ATOM 3552 CA ILE A 780 -4.490 27.417 34.527 1.00 20.60 C

ANISOU 3552 CA ILE A 780 2888 2483 2455 215 -910 -727 C

ATOM 3553 CB ILE A 780 -5.960 27.714 34.866 1.00 35.95 C

ANISOU 3553 CB ILE A 780 4848 4452 4360 187 -844 -749 C

ATOM 3554 CG2 ILE A 780 -6.542 28.736 33.887 1.00 33.78 C

ANISOU 3554 CG2 ILE A 780 4458 4181 4196 158 -819 -741 C

ATOM 3555 CGI ILE A 780 -6.775 26.417 34.892 1.00 28.76 C

ANISOU 3555 CGI ILE A 780 3978 3573 3379 154 -799 -702 C

ATOM 3556 CD 1 ILE A 780 -6.848 25.732 33.557 1.00 24.56 C

ANISOU 3556 CD 1 ILE A 780 3355 3057 2921 117 -786 -624 C

ATOM 3557 C ILE A 780 -3.678 28.712 34.659 1.00 21.93 C

ANISOU 3557 C ILE A 780 3032 2621 2680 251 -958 -776 C

ATOM 3558 O ILE A 780 -3.206 29.263 33.661 1.00 21.55 O

ANISOU 3558 O ILE A 780 2893 2563 2732 248 -971 -754 O

ATOM 3559 N ASN A 781 -3.520 29.195 35.884 1.00 24.40 N

ANISOU 3559 N ASN A 781 3429 2917 2924 283 -981 -843 N

ATOM 3560 CA ASN A 781 -2.779 30.444 36.116 1.00 28.40 C ANISOU 3560 CA ASN A 781 3919 3392 3479 318 -1031 -896 C

ATOM 3561 CB ASN A 781 -2.776 30.812 37.608 1.00 24.79 C

ANISOU 3561 CB ASN A 781 3575 2921 2924 351 -1041 -974 C

ATOM 3562 CG ASN A 781 -4.152 31.210 38.118 1.00 28.88 C ANISOU 3562 CG ASN A 781 4124 3450 3399 337 -964 -1022 C

ATOM 3563 OD1 ASN A 781 -5.054 31.514 37.338 1.00 26.89 O ANISOU 3563 OD1 ASN A 781 3797 3207 3211 304 -915 -1006 O

ATOM 3564 ND2 ASN A 781 -4.319 31.205 39.435 1.00 34.93 N ANISOU 3564 ND2 ASN A 781 5004 4213 4056 363 -946 -1082 N

ATOM 3565 C ASN A 781 -1.342 30.421 35.577 1.00 33.17 C

ANISOU 3565 C ASN A 781 4487 3972 4145 342 -1096 -870 C

ATOM 3566 O ASN A 781 -0.856 31.419 35.040 1.00 25.21 O

ANISOU 3566 O ASN A 781 3410 2944 3224 353 -1124 -880 O

ATOM 3567 N ARG A 782 -0.668 29.282 35.720 1.00 27.87 N ANISOU 3567 N ARG A 782 3863 3297 3430 351 -1118 -841 N

ATOM 3568 CA ARG A 782 0.727 29.155 35.303 1.00 22.45 C

ANISOU 3568 CA ARG A 782 3156 2580 2794 377 -1173 -826 C

ATOM 3569 CB ARG A 782 1.437 28.084 36.140 1.00 25.06 C

ANISOU 3569 CB ARG A 782 3582 2895 3045 398 -1213 -827 C ATOM 3570 CG ARG A 782 1.596 28.456 37.613 1.00 25.81 C

ANISOU 3570 CG ARG A 782 3781 2977 3049 426 -1250 -886 C

ATOM 3571 CD ARG A 782 2.125 27.293 38.438 1.00 32.21 C

ANISOU 3571 CD ARG A 782 4690 3774 3776 437 -1283 -877 C

ATOM 3572 NE ARG A 782 3.361 26.744 37.887 1.00 43.32 N

ANISOU 3572 NE ARG A 782 6071 5150 5237 452 -1332 -850 N

ATOM 3573 CZ ARG A 782 4.579 27.177 38.200 1.00 51.09 C

ANISOU 3573 CZ ARG A 782 7072 6099 6241 488 -1400 -876 C ATOM 3574 NHl ARG A 782 4.731 28.173 39.066 1.00 43.33 N ANISOU 3574 NHl ARG A 782 6132 5106 5226 511 -1431 -929 N ATOM 3575 NH2 ARG A 782 5.647 26.613 37.645 1.00 42.57 N ANISOU 3575 NH2 ARG A 782 5969 4993 5213 500 -1436 -854 N

ATOM 3576 C ARG A 782 0.877 28.838 33.815 1.00 19.58 C

ANISOU 3576 C ARG A 782 2697 2223 2520 353 -1143 -769 C

ATOM 3577 O ARG A 782 1.988 28.743 33.300 1.00 27.07 O

ANISOU 3577 O ARG A 782 3621 3147 3515 370 -1175 -760 O

ATOM 3578 N GLY A 783 -0.241 28.655 33.120 1.00 20.95 N

ANISOU 3578 N GLY A 783 2819 2428 2712 311 -1078 -734 N

ATOM 3579 CA GLY A 783 -0.172 28.300 31.713 1.00 15.68 C

ANISOU 3579 CA GLY A 783 2071 1769 2116 282 -1040 -681 C

ATOM 3580 C GLY A 783 0.345 26.889 31.465 1.00 14.98 C

ANISOU 3580 C GLY A 783 2010 1679 2004 280 -1040 -651 C

ATOM 3581 O GLY A 783 0.712 26.542 30.339 1.00 25.21 O

ANISOU 3581 O GLY A 783 3251 2975 3351 265 -1016 -619 O

ATOM 3582 N GLN A 784 0.371 26.071 32.513 1.00 18.95 N

ANISOU 3582 N GLN A 784 2599 2177 2423 294 -1066 -663 N

ATOM 3583 CA GLN A 784 0.768 24.666 32.395 1.00 18.97 C

ANISOU 3583 CA GLN A 784 2633 2173 2402 291 -1073 -636 C

ATOM 3584 CB GLN A 784 0.838 24.000 33.780 1.00 27.14 C

ANISOU 3584 CB GLN A 784 3778 3194 3338 309 -1113 -656 C

ATOM 3585 CG GLN A 784 1.879 24.627 34.709 1.00 42.08 C

ANISOU 3585 CG GLN A 784 5725 5053 5210 355 -1183 -704 C

ATOM 3586 CD GLN A 784 1.850 24.080 36.136 1.00 52.80 C

ANISOU 3586 CD GLN A 784 7201 6400 6458 368 -1216 -724 C ATOM 3587 OE1 GLN A 784 2.843 24.173 36.859 1.00 77.03 O

ANISOU 3587 OE1 GLN A 784 10325 9438 9505 401 -1279 -753 O ATOM 3588 NE2 GLN A 784 0.715 23.517 36.548 1.00 34.14 N

ANISOU 3588 NE2 GLN A 784 4880 4065 4025 339 -1173 -709 N

ATOM 3589 C GLN A 784 -0.164 23.887 31.466 1.00 21.90 C

ANISOU 3589 C GLN A 784 2957 2575 2787 244 -1007 -586 C

ATOM 3590 O GLN A 784 -1.362 24.161 31.404 1.00 15.43 O ANISOU 3590 O GLN A 784 2120 1787 1957 213 -959 -572 O

ATOM 3591 N ILE A 785 0.400 22.921 30.741 1.00 10.77 N

ANISOU 3591 N ILE A 785 1731 1405 956 79 22 -161 N

ATOM 3592 CA ILE A 785 -0.333 22.184 29.712 1.00 14.32 C

ANISOU 3592 CA ILE A 785 2171 1849 1419 91 15 -144 C